Page last updated: 2024-12-09

omapatrilat

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Description

omapatrilat: structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID656629
CHEMBL ID289556
CHEBI ID135660
SCHEMBL ID130098
MeSH IDM0276976

Synonyms (47)

Synonym
(4s,7s,10as)-4-((s)-2-mercapto-3-phenylpropanamido)-5-oxo-octahydro-2h-pyrido[2,1-b][1,3]thiazepine-7-carboxylic acid
(4s,6s,9as)-6-((s)-2-mercapto-3-phenyl-propionylamino)-5-oxo-octahydro-9-thia-4a-aza-benzocycloheptene-4-carboxylic acid
bdbm50073120
vanlev
bms-186716
octahydro-4-((2-mercapto-1-oxo-3-phenylpropyl)amino)-5-oxo-7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid
omapatrilat
omapatrilat (jan/usan/inn)
167305-00-2
bms 186716
D01970
(4s,7s,10as)-octahydro-4-((s)-alpha-mercaptohydrocinnamamido)-5-oxo-7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid
bms-186716-01
(4s-(4alpha(r*),7alpha,10abeta))-octahydro-4-((2-mercapto-1-oxo-3-phenylpropyl)amino)-5-oxo-7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid
7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid, octahydro-4-((2-mercapto-1-oxo-3-phenylpropyl)amino)-5-oxo-, (4s-(4alpha(r*),7alpha,10abeta))-
7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid, octahydro-4-(((2s)-2-mercapto-1-oxo-3-phenylpropyl)amino)-5-oxo-, (4s,7s,10as)-
omapatrilat [usan]
CHEBI:135660
CHEMBL289556 ,
(4s,7s,10as)-5-oxo-4-[[(2s)-3-phenyl-2-sulfanylpropanoyl]amino]-2,3,4,7,8,9,10,10a-octahydropyrido[2,1-b][1,3]thiazepine-7-carboxylic acid
unii-36nli90e7t
36nli90e7t ,
omapatrilat [usan:inn:ban]
omapatrilat [mi]
omapatrilat [mart.]
omapatrilat [vandf]
(4s-(4.alpha.(r*),7.alpha.,10a.beta.))-octahydro-4-((2-mercapto-1-oxo-3-phenylpropyl)amino)-5-oxo-7h-pyrido(2,1-b)(1,3)thiazepine-7-carboxylic acid
(4s,7s,10as)-octahydro-4-[(s)-alpha-mercaptohydrocinnamamido]-5-oxo-7h-pyrido[2,1-b][1,3]thiazepine-7-carboxylic acid
omapatrilat [jan]
omapatrilat [who-dd]
omapatrilat [inn]
DB00886
omapatrilate
SCHEMBL130098
DTXSID80168273
omapatrilat, >=98% (hplc)
(4s,7s,10as)-4-((s)-2-mercapto-3-phenylpropanamido)-5-oxooctahydro-2h-pyrido[2,1-b][1,3]thiazepine-7-carboxylic acid
CS-6369
HY-18208
omapatrylate
159317-63-2
Q7089596
NCGC00509984-01
ft8 ,
(4s,7s,10as)-4-((s)-2-mercapto-3-phenylpropanamido)-5-oxooctahydro-7h-pyrido[2,1-b][1,3]thiazepine-7-carboxylic acid
MS-27025
AKOS040742333

Research Excerpts

Overview

Omapatrilat (OMP) is a novel mixed inhibitor of angiotensin-converting enzyme (ACE) and neutral endopeptidase 24.11 (NEP), the enzyme that metabolizes natriuretic peptides. Omapatrillat appears to be a safe, well-tolerated and effective antihypertensive in humans.

ExcerptReferenceRelevance
"Omapatrilat is a potent vasopeptidase inhibitor that significantly inhibits tissue ACE and NEP, with the degree of inhibition varying according to the enzyme and the tissue under assessment."( Differential tissue and enzyme inhibitory effects of the vasopeptidase inhibitor omapatrilat in the rat.
Burrell, LM; Casley, DJ; Dean, RG; Hubner, RA; Johnston, CI; Kubota, E, 2003
)
1.27
"Omapatrilat (OMP) is a novel mixed inhibitor of angiotensin-converting enzyme (ACE) and neutral endopeptidase 24.11 (NEP), the enzyme that metabolizes natriuretic peptides. "( Cardiac and renal effects of omapatrilat, a vasopeptidase inhibitor, in rats with experimental congestive heart failure.
Abassi, ZA; Golomb, E; Hoffman, A; Karram, T; Winaver, J; Yahia, A; Zeid, S, 2005
)
2.06
"Omapatrilat is a dual angiotensin converting enzyme and neutral endopeptidase inhibitor. "( [Omapatrilat--new drug for patients with hypertension and heart failure].
Dzielska-Olczak, M, 2005
)
2.68
"Omapatrilat appears to be a safe, well-tolerated and effective antihypertensive in humans."( Vasopeptidase inhibition: a new concept in blood pressure management.
Burnett, JC, 1999
)
1.02
"Omapatrilat is a member of the new drug class of vasopeptidase inhibitors that may offer benefit in the treatment of heart failure (HF) through simultaneous inhibition of angiotensin-converting enzyme and neutral endopeptidase. "( Beneficial renal and hemodynamic effects of omapatrilat in mild and severe heart failure.
Espiner, EA; Frampton, CM; Nicholls, MG; Powell, JD; Rademaker, MT; Richards, AM; Troughton, RW; Yandle, TG, 2000
)
2.01
"Omapatrilat is a potent vasopeptidase inhibitor, and its antihypertensive effects are associated with inhibition of NEP and ACE at the tissue level and beneficial effects on cardiovascular structure."( Antihypertensive and antihypertrophic effects of omapatrilat in SHR.
Burrell, LM; Droogh, J; Farina, NK; Johnston, CI; Man in't Veld, O; Rockell, MD, 2000
)
1.28
"Omapatrilat is a single molecule that simultaneously inhibits neutral endopeptidase and angiotensin-converting enzyme, thus preserving vasodilator peptides and inhibiting production of the vasoconstrictor angiotensin II."( Effects of age and gender on the pharmacodynamics of omapatrilat in healthy volunteers.
Davis, KD; Ferreira, IM; Hammett, JL; Hutman, HW; Liao, W; Manning, J; Meier, A; Vesterqvist, O,
)
1.1
"Omapatrilat is a newly developed vasopeptidase inhibitor that inhibits both angiotensin-converting enzyme (ACE) and neutral endopeptidase and has potent antihypertensive efficacy. "( The cardiovascular actions of omapatrilat in spontaneously hypertensive rats.
Atamas, N; Dong, Y; Liao, WC; Shaffer, E; Wei, C; Zhou, H, 2001
)
2.04

Effects

Omapatrilat has a substantial anti-atherosclerotic effect, which can be related not only to BP reduction but also to its ability to reduce oxidative stress in atherosclerosis E0 mice. Omapatrillat, a VPI, has a greater protective effect on BK metabolism than that of a pure ACE inhibitor.

Omapatrilat has potent enzymatic inhibitory effects on the angiotensin-converting enzyme and neutral endopeptidase. The drug has a substantial anti-atherosclerotic effect, which can be related not only to BP reduction but also to its ability to reduce oxidative stress.

ExcerptReferenceRelevance
"Omapatrilat has a substantial anti-atherosclerotic effect, which can be related not only to BP reduction but also to its ability to reduce oxidative stress in atherosclerotic E0 mice."( Omapatrilat decreased macrophage oxidative status and atherosclerosis progression in atherosclerotic apolipoprotein E-deficient mice.
Aviram, M; Coleman, R; Hamoud, S; Hayek, T; Kaplan, M; Keidar, S; Pavlotzky, E, 2004
)
3.21
"Omapatrilat, a VPI, has a greater protective effect on BK metabolism than that of a pure ACE inhibitor."( Protective effect of omapatrilat, a vasopeptidase inhibitor, on the metabolism of bradykinin in normal and failing human hearts.
Adam, A; Blais, C; Fortin, D; Molinaro, G; Rouleau, JL, 2000
)
1.35
"Omapatrilat has potent enzymatic inhibitory effects on the angiotensin-converting enzyme and neutral endopeptidase. "( Omapatrilat induces profound renal vasodilation but does not affect coronary hemodynamics.
Frohlich, ED; Slama, M; Susic, D; Varagic, J, 2003
)
3.2
"Omapatrilat has a substantial anti-atherosclerotic effect, which can be related not only to BP reduction but also to its ability to reduce oxidative stress in atherosclerotic E0 mice."( Omapatrilat decreased macrophage oxidative status and atherosclerosis progression in atherosclerotic apolipoprotein E-deficient mice.
Aviram, M; Coleman, R; Hamoud, S; Hayek, T; Kaplan, M; Keidar, S; Pavlotzky, E, 2004
)
3.21
"Omapatrilat has the potential to be an effective, broad spectrum antihypertensive agent."( Effects of omapatrilat in low, normal, and high renin experimental hypertension.
Asaad, MM; Fox, M; Panchal, BC; Robl, JA; Schaeffer, TR; Trippodo, NC, 1998
)
1.41
"Omapatrilat, a VPI, has a greater protective effect on BK metabolism than that of a pure ACE inhibitor."( Protective effect of omapatrilat, a vasopeptidase inhibitor, on the metabolism of bradykinin in normal and failing human hearts.
Adam, A; Blais, C; Fortin, D; Molinaro, G; Rouleau, JL, 2000
)
1.35
"Omapatrilat has consistently shown efficacy in decreasing both systolic and diastolic blood pressure to a similar or greater extent than either lisinopril or amlodipine; however, systolic pressure is more responsive to omapatrilat treatment than diastolic pressure."( Omapatrilat: a unique new agent for the treatment of cardiovascular disease.
Anderson, JR; Nawarskas, JJ,
)
2.3

Actions

Omapatrilat induced an increase in postdose plasma atrial natriuretic peptide levels (p<0.01) in high-dose groups consistent with endopeptidase 24.11 inhibition.

ExcerptReferenceRelevance
"Omapatrilat induced an increase in postdose plasma atrial natriuretic peptide levels (p<0.01) in the high dose groups, with a reduction in predose plasma brain natriuretic peptide (p<0.001) and epinephrine (p<0.01) levels after 12 weeks of therapy."( The clinical, cardiac, renal, arterial and neurohormonal effects of omapatrilat, a vasopeptidase inhibitor, in patients with chronic heart failure.
Crozier, IG; Garlick, AH; Ikram, H; McClean, DR; Nicholls, MG; Richards, AM, 2000
)
1.26
"Omapatrilat induced an increase in postdose plasma atrial natriuretic peptide levels (30 +/- 11 vs -2 +/- 7 pmol/L, p < 0.01) in high-dose groups consistent with endopeptidase 24.11 inhibition."( Effects of omapatrilat on systemic arterial function in patients with chronic heart failure.
Crozier, IG; Garlick, AH; Ikram, H; McClean, DR, 2001
)
1.42

Treatment

Omapatrilat treatment significantly reduced left ventricular hypertrophy and improved endothelial function in carotid arteries from male SHRSP by NO-dependent mechanisms. Omapatrillat treatment normalized the BNP and reduced the BP by 45 mm Hg in the NX rats.

ExcerptReferenceRelevance
"Omapatrilat treatment normalized the BNP and reduced the BP by 45 mm Hg in the NX rats."( Vasopeptidase Inhibition Corrects the Structure and Function of the Small Arteries in Experimental Renal Insufficiency.
Eräranta, A; Haltia, O; Jokihaara, J; Mustonen, J; Nordhausen, K; Pörsti, I; Ruskoaho, H; Rysä, J; Tikkanen, I; Törmänen, S, 2015
)
1.14
"Omapatrilat treatment reduced BP, normalized volume overload, improved vasorelaxation and corrected the dimensions and passive elastic properties of the small arteries in the NX rats. "( Vasopeptidase Inhibition Corrects the Structure and Function of the Small Arteries in Experimental Renal Insufficiency.
Eräranta, A; Haltia, O; Jokihaara, J; Mustonen, J; Nordhausen, K; Pörsti, I; Ruskoaho, H; Rysä, J; Tikkanen, I; Törmänen, S, 2015
)
1.86
"Omapatrilat treatment did not affect weight or plasma glucose levels."( Omapatrilat, an angiotensin-converting enzyme and neutral endopeptidase inhibitor, attenuates early atherosclerosis in diabetic and in nondiabetic low-density lipoprotein receptor-deficient mice.
Cohen, H; Dvir, A; Harats, D; Levkovietz, H; Levy, Z; Ravid, M; Rhachmani, R; Shaish, A; Trestman, S,
)
2.3
"The Omapatrilat-treated mice serum susceptibility to lipid peroxidation was reduced by up to 21%, and their serum paraoxonase activity was increased by up to 24%, compared with placebo-treated mice."( Omapatrilat decreased macrophage oxidative status and atherosclerosis progression in atherosclerotic apolipoprotein E-deficient mice.
Aviram, M; Coleman, R; Hamoud, S; Hayek, T; Kaplan, M; Keidar, S; Pavlotzky, E, 2004
)
2.25
"Two omapatrilat-treated subjects experienced angioedema with airway compromise, which was successfully treated."( Omapatrilat and enalapril in patients with hypertension: the Omapatrilat Cardiovascular Treatment vs. Enalapril (OCTAVE) trial.
Black, HR; Henry, D; Kostis, JB; Levy, E; Packer, M; Schmieder, R, 2004
)
2.25
"Omapatrilat treatment significantly reduced left ventricular hypertrophy and improved endothelial function in carotid arteries from male SHRSP by NO-dependent mechanisms. "( Comparison of the effects of omapatrilat and irbesartan/hydrochlorothiazide on endothelial function and cardiac hypertrophy in the stroke-prone spontaneously hypertensive rat: sex differences.
Beattie, E; Dominiczak, AF; Graham, D; Hamilton, C; Spiers, A, 2004
)
2.06
"Omapatrilat (OMA) treatment relieved myocardial lesions and improved cardiac function."( Changes in production and metabolism of brain natriuretic peptide in rats with myocardial necrosis.
Cai, DY; Geng, B; Jiang, HF; Jiang, W; Pan, CS; Qi, YF; Tang, CS, 2005
)
1.05
"Omapatrilat treatment reduced MI size and resulted in beneficial ventricular remodelling as reflected by a reduction in cardiac dimensions by echocardiography, and LV and right ventricular hypertrophy, which resulted in borderline hemodynamic improvement."( Effects of the vasopeptidase inhibitor omapatrilat on peri- and postmyocardial infarction in Zucker lean rats.
Adam, A; Lapointe, N; Lou, I; Marcotte, F; Nguyen, QT; Parker, TG; Rouleau, JL; Tsoporis, JN, 2005
)
1.32
"Omapatrilat treatment improved endothelium-dependent relaxation of resistance arteries as elicited by acetylcholine (10(-5) mol/L) but had no significant effect on endothelium-independent relaxation produced by a nitric oxide donor (sodium nitroprusside)."( Vasopeptidase inhibition has potent effects on blood pressure and resistance arteries in stroke-prone spontaneously hypertensive rats.
Intengan, HD; Schiffrin, EL, 2000
)
1.03
"Both omapatrilat and enalapril treatments of MI rats significantly increased cardiac BK concentrations compared with the sham-operated group (P < 0.05)."( Effects of the vasopeptidase inhibitor omapatrilat on cardiac endogenous kinins in rats with acute myocardial infarction.
Adam, A; Blais, C; Clément, R; Geadah, D; Gervais, N; Lapointe, N; Rouleau, JL, 2001
)
1.04
"Omapatrilat treatment of the SN-salt rats significantly decreased the mean arterial pressure to 123+/-7 mm Hg and significantly reduced the heart-to-body weight ratio."( Omapatrilat in subtotal nephrectomy-salt hypertension: role of calcitonin gene-related peptide.
DiPette, DJ; Supowit, SC; Wang, DH; Zhao, H, 2001
)
2.47
"Both omapatrilat and captopril treatments improve early (4 days) post-MI survival when started 4 h post-MI."( Effects of captopril and omapatrilat on early post-myocardial infarction survival and cardiac hemodynamics in rats: interaction with cardiac cytokine expression.
Adam, A; Bachvarov, DR; Blais, C; Clément, R; Lapointe, N; Rouleau, JL, 2002
)
1.07
"Omapatrilat and CGS treatment increased lumen diameter and decreased media width and media/lumen ratio of small arteries of DOCA-salt rats (P < 0.05)."( Comparison of angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP) and dual ACE/NEP inhibition on blood pressure and resistance arteries of deoxycorticosterone acetate-salt hypertensive rats.
Pu, Q; Schiffrin, EL; Touyz, RM, 2002
)
1.04
"Treatment with omapatrilat or lisinopril reduced SAP in HT (P <0.05) similarly by about 10%."( Comparison of the cardiovascular protection by omapatrilat and lisinopril treatments in DOCA-salt hypertension.
de Champlain, J; Demeilliers, B; El Midaoui, A; Lamontagne, D; Laplante, MA; Millette, E; Moreau, P; Wu, R, 2003
)
0.92
"Rats treated with omapatrilat and captopril had reduced cardiac BNP mRNA levels and less myocardial fibrosis by comparison with the vehicle-treated rats."( Effect of vasopeptidase inhibitor omapatrilat on cardiomyocyte apoptosis and ventricular remodeling in rat myocardial infarction.
Bäcklund, T; Eriksson, A; Grönholm, T; Laine, M; Lakkisto, P; Nieminen, MS; Palojoki, E; Saraste, A; Tikkanen, I; Voipio-Pulkki, LM; Vuolteenaho, O, 2003
)
0.92
"Treatment with omapatrilat inhibits atherogenesis in diabetic as well as nondiabetic LDL receptor-deficient mice despite an increase in plasma lipids, suggesting a direct effect on the arterial wall."( Omapatrilat, an angiotensin-converting enzyme and neutral endopeptidase inhibitor, attenuates early atherosclerosis in diabetic and in nondiabetic low-density lipoprotein receptor-deficient mice.
Cohen, H; Dvir, A; Harats, D; Levkovietz, H; Levy, Z; Ravid, M; Rhachmani, R; Shaish, A; Trestman, S,
)
1.91
"Treatment with omapatrilat resulted in improved early (24 h) and late (38 days) survival following MI (50% to 67%, P=0.023, and 44% to 59%, P=0.045, respectively). "( Effects of the vasopeptidase inhibitor omapatrilat on peri- and postmyocardial infarction in Zucker lean rats.
Adam, A; Lapointe, N; Lou, I; Marcotte, F; Nguyen, QT; Parker, TG; Rouleau, JL; Tsoporis, JN, 2005
)
0.95
"Treatment with omapatrilat has a higher tendency towards preventing death and worsening heart failure."( [Omapatrilat--new drug for patients with hypertension and heart failure].
Dzielska-Olczak, M, 2005
)
1.58

Toxicity

ExcerptReferenceRelevance
" Adverse events, serious adverse events, and discontinuations attributed to adverse events were infrequent."( Efficacy and safety of omapatrilat with hydrochlorothiazide for the treatment of hypertension in subjects nonresponsive to hydrochlorothiazide alone.
Barbosa, JA; Ferdinand, K; Kushnir, E; Lewin, A; Saini, R; Yellen, L, 2001
)
0.62
" Thus, omapatrilat administered orally to patients with heart failure was safe and well tolerated and resulted in improved hemodynamic performance."( Effects of omapatrilat on hemodynamics and safety in patients with heart failure.
Bilsker, M; Eng, C; Heywood, JT; Iteld, BJ; Klapholz, M; Niederman, AL; Ponce, GA; Synhorst, D; Thomas, I, 2001
)
1.16

Pharmacokinetics

The pharmacokinetic and pharmacodynamic effects of omapatrilat are consistent with once-daily dosing. This article outlines the pharmacodynamics effects of the vasopeptidase inhibitor omap atrilat on biomarkers of NEP and ACE activity in humans.

ExcerptReferenceRelevance
" Pharmacokinetic parameters were determined from plasma omapatrilat concentrations."( Omapatrilat in patients with hepatic cirrhosis. Pharmacodynamics and pharmacokinetics.
Ge, G; Jemal, M; Malhotra, B; Mangold, B; Manning, J; O'Grady, P; Vesterqvist, O, 2001
)
2
" This article outlines the pharmacodynamic effects of the vasopeptidase inhibitor omapatrilat on biomarkers of NEP and ACE activity in humans."( Effects of omapatrilat on pharmacodynamic biomarkers of neutral endopeptidase and Angiotensin-converting enzyme activity in humans.
Reeves, RA; Vesterqvist, O, 2001
)
0.93
" Clinical pharmacokinetic parameters were similar in both groups after intravenous dosing, but maximum concentration and area under the concentration-time curve were elevated in CHF patients compared with controls after oral dosing."( Pharmacodynamics and pharmacokinetics of omapatrilat in heart failure.
Cohen, M; Delaney, C; Jemal, M; Klapholz, M; Kollia, GD; Kostis, JB; Liao, WC; Manning, JA; Vesterqvist, O, 2001
)
0.58
" The pharmacokinetic and pharmacodynamic effects of omapatrilat are consistent with once-daily dosing."( Pharmacokinetics and pharmacodynamics of the vasopeptidase inhibitor, omapatrilat in healthy subjects.
Delaney, C; Ferreira, I; Ford, N; Jemal, M; Liao, WC; Swanson, B; Uderman, H; Vesterqvist, O, 2003
)
0.8

Bioavailability

ExcerptReferenceRelevance
"The objective of this study was to determine the absolute oral bioavailability and disposition of omapatrilat."( Oral bioavailability and disposition of [14C]omapatrilat in healthy subjects.
Behr, D; Cohen, MB; Iyer, RA; Kaul, S; Knupp, CA; Liao, WC; Malhotra, BK; Mitroka, JG; Soucek, KM, 2001
)
0.79
" Endothelial function [basal nitric oxide (NO) bioavailability and stimulated NO release] was examined in carotid arteries using organ bath pharmacology and in mesenteric resistance arteries using wire myography."( Comparison of the effects of omapatrilat and irbesartan/hydrochlorothiazide on endothelial function and cardiac hypertrophy in the stroke-prone spontaneously hypertensive rat: sex differences.
Beattie, E; Dominiczak, AF; Graham, D; Hamilton, C; Spiers, A, 2004
)
0.61
" MO-nanoparticles can be an interesting system to increase the oral bioavailability of drugs."( Evaluation of the enhanced oral effect of omapatrilat-monolein nanoparticles prepared by the emulsification-diffusion method.
Ganem-Quintanar, A; Martínez, AL; Navarrete-Rodríguez, M; Quintanar-Guerrero, D; Rodríguez-Romo, S; Tamayo-Esquivel, D,
)
0.4

Dosage Studied

Omapatrilat (100 micromol/kg/day) persistently lowered systolic blood pressure (tail cuff) in spontaneously hypertensive rats during 11 days of treatment. At 24 h after dosing on day 12, mean arterial pressure (aortic catheter) was lower (P < . urinary excretion rates of Ang I and Ang-(1-7) but not Ang II increased significantly throughout the dosing period.

ExcerptRelevanceReference
" After oral administration, omapatrilat (100 micromol/kg/day) persistently lowered systolic blood pressure (tail cuff) in spontaneously hypertensive rats during 11 days of treatment; at 24 h after dosing on day 12, mean arterial pressure (aortic catheter) was lower (P < ."( Effects of omapatrilat in low, normal, and high renin experimental hypertension.
Asaad, MM; Fox, M; Panchal, BC; Robl, JA; Schaeffer, TR; Trippodo, NC, 1998
)
0.98
" Plasma atrial and brain natriuretic peptide and cGMP levels were stable acutely (P=NS), while brain natriuretic peptide increased after repeated dosing in severe HF (P<0."( Beneficial renal and hemodynamic effects of omapatrilat in mild and severe heart failure.
Espiner, EA; Frampton, CM; Nicholls, MG; Powell, JD; Rademaker, MT; Richards, AM; Troughton, RW; Yandle, TG, 2000
)
0.57
" This study describes the plasma profile along with isolation and identification of urinary metabolites of omapatrilat from subjects dosed orally with 50 mg of [(14)C]omapatrilat."( Metabolism of [(14)C]omapatrilat, a sulfhydryl-containing vasopeptidase inhibitor in humans.
Bonacorsi, S; Iyer, RA; Kripalani, K; Malhotra, B; Mitroka, J; Rinehart, JK; Roongta, VA; Waller, SC, 2001
)
0.84
"These results suggest, based on findings in otherwise healthy cirrhotic subjects, that no adjustment of standard dosing regimens is indicated for hypertensive patients with mild to moderate cirrhosis."( Omapatrilat in patients with hepatic cirrhosis. Pharmacodynamics and pharmacokinetics.
Ge, G; Jemal, M; Malhotra, B; Mangold, B; Manning, J; O'Grady, P; Vesterqvist, O, 2001
)
1.75
" Additionally, by 2 hours after dosing with omapatrilat 25 and 50 mg, a trend in peak increases from baseline in plasma atrial natriuretic peptide (twofold) and cyclic guanosine monophosphate (nearly twofold) was observed."( Effects of omapatrilat on hemodynamics and safety in patients with heart failure.
Bilsker, M; Eng, C; Heywood, JT; Iteld, BJ; Klapholz, M; Niederman, AL; Ponce, GA; Synhorst, D; Thomas, I, 2001
)
0.96
" The pharmacokinetics of omapatrilat are compatible with once-daily dosing and a duration of antihypertensive efficacy of more than 24 hours."( Omapatrilat: a unique new agent for the treatment of cardiovascular disease.
Anderson, JR; Nawarskas, JJ,
)
1.88
" Angiotensin-converting enzyme activity was > 90% inhibited at 4 hours after dosing and remained approximately 60% to 70% inhibited at 24 hours after dosing."( Pharmacodynamics and pharmacokinetics of omapatrilat in heart failure.
Cohen, M; Delaney, C; Jemal, M; Klapholz, M; Kollia, GD; Kostis, JB; Liao, WC; Manning, JA; Vesterqvist, O, 2001
)
0.58
" In contrast, urinary excretion rates of Ang I and Ang-(1-7) but not Ang II increased significantly throughout the dosing period of subjects who were given omapatrilat, whereas the smaller antihypertensive response produced by lisinopril had a smaller and transient effect on increasing urinary excretion rates of Ang-(1-7)."( Effects of omapatrilat on the renin-angiotensin system in salt-sensitive hypertension.
Brosnihan, B; Campese, VM; Chappell, MC; Ferrario, CM; Grim, CE; Liao, WC; Ruddy, MC; Smith, RD; Vesterqvist, O, 2002
)
0.9
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Drug Classes (1)

ClassDescription
dipeptideAny molecule that contains two amino-acid residues connected by peptide linkages.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Protein Targets (7)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Amyloid-beta precursor proteinHomo sapiens (human)IC50 (µMol)0.19950.00053.889510.0000AID1515584
NeprilysinRattus norvegicus (Norway rat)IC50 (µMol)0.00830.00100.17022.3000AID147231; AID147361; AID147368; AID1607322
NeprilysinHomo sapiens (human)IC50 (µMol)0.00020.00020.54226.7000AID1515581
NeprilysinHomo sapiens (human)Ki0.00900.00150.00440.0090AID444547
Angiotensin-converting enzyme Homo sapiens (human)IC50 (µMol)0.00100.00010.533610.0000AID1423283; AID1423284; AID1515583
Angiotensin-converting enzyme Homo sapiens (human)Ki0.00380.00000.82557.5000AID1423287; AID1423288; AID444546; AID444547
Angiotensin-converting enzymeOryctolagus cuniculus (rabbit)IC50 (µMol)0.00530.00001.612910.0000AID37645; AID37663; AID37787
Type-1 angiotensin II receptorHomo sapiens (human)Ki10.00000.00020.18374.7000AID1515578
Squalene synthaseRattus norvegicus (Norway rat)Ki10.00000.00500.65582.6000AID1515578
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (170)

Processvia Protein(s)Taxonomy
regulation of gene expressionAmyloid-beta precursor proteinHomo sapiens (human)
cognitionAmyloid-beta precursor proteinHomo sapiens (human)
G2/M transition of mitotic cell cycleAmyloid-beta precursor proteinHomo sapiens (human)
microglial cell activationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of protein phosphorylationAmyloid-beta precursor proteinHomo sapiens (human)
suckling behaviorAmyloid-beta precursor proteinHomo sapiens (human)
astrocyte activation involved in immune responseAmyloid-beta precursor proteinHomo sapiens (human)
regulation of translationAmyloid-beta precursor proteinHomo sapiens (human)
protein phosphorylationAmyloid-beta precursor proteinHomo sapiens (human)
intracellular copper ion homeostasisAmyloid-beta precursor proteinHomo sapiens (human)
endocytosisAmyloid-beta precursor proteinHomo sapiens (human)
response to oxidative stressAmyloid-beta precursor proteinHomo sapiens (human)
cell adhesionAmyloid-beta precursor proteinHomo sapiens (human)
regulation of epidermal growth factor-activated receptor activityAmyloid-beta precursor proteinHomo sapiens (human)
Notch signaling pathwayAmyloid-beta precursor proteinHomo sapiens (human)
axonogenesisAmyloid-beta precursor proteinHomo sapiens (human)
learning or memoryAmyloid-beta precursor proteinHomo sapiens (human)
learningAmyloid-beta precursor proteinHomo sapiens (human)
mating behaviorAmyloid-beta precursor proteinHomo sapiens (human)
locomotory behaviorAmyloid-beta precursor proteinHomo sapiens (human)
axo-dendritic transportAmyloid-beta precursor proteinHomo sapiens (human)
cholesterol metabolic processAmyloid-beta precursor proteinHomo sapiens (human)
negative regulation of cell population proliferationAmyloid-beta precursor proteinHomo sapiens (human)
adult locomotory behaviorAmyloid-beta precursor proteinHomo sapiens (human)
visual learningAmyloid-beta precursor proteinHomo sapiens (human)
regulation of gene expressionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of gene expressionAmyloid-beta precursor proteinHomo sapiens (human)
negative regulation of gene expressionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of peptidyl-threonine phosphorylationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of G2/M transition of mitotic cell cycleAmyloid-beta precursor proteinHomo sapiens (human)
microglia developmentAmyloid-beta precursor proteinHomo sapiens (human)
axon midline choice point recognitionAmyloid-beta precursor proteinHomo sapiens (human)
neuron remodelingAmyloid-beta precursor proteinHomo sapiens (human)
dendrite developmentAmyloid-beta precursor proteinHomo sapiens (human)
regulation of Wnt signaling pathwayAmyloid-beta precursor proteinHomo sapiens (human)
extracellular matrix organizationAmyloid-beta precursor proteinHomo sapiens (human)
forebrain developmentAmyloid-beta precursor proteinHomo sapiens (human)
neuron projection developmentAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of chemokine productionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of interleukin-1 beta productionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of interleukin-6 productionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of tumor necrosis factor productionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of peptidyl-serine phosphorylationAmyloid-beta precursor proteinHomo sapiens (human)
ionotropic glutamate receptor signaling pathwayAmyloid-beta precursor proteinHomo sapiens (human)
regulation of multicellular organism growthAmyloid-beta precursor proteinHomo sapiens (human)
negative regulation of neuron differentiationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of glycolytic processAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of mitotic cell cycleAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of transcription by RNA polymerase IIAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of JNK cascadeAmyloid-beta precursor proteinHomo sapiens (human)
astrocyte activationAmyloid-beta precursor proteinHomo sapiens (human)
regulation of long-term neuronal synaptic plasticityAmyloid-beta precursor proteinHomo sapiens (human)
collateral sprouting in absence of injuryAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of inflammatory responseAmyloid-beta precursor proteinHomo sapiens (human)
regulation of peptidyl-tyrosine phosphorylationAmyloid-beta precursor proteinHomo sapiens (human)
regulation of synapse structure or activityAmyloid-beta precursor proteinHomo sapiens (human)
synapse organizationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of calcium-mediated signalingAmyloid-beta precursor proteinHomo sapiens (human)
neuromuscular process controlling balanceAmyloid-beta precursor proteinHomo sapiens (human)
synaptic assembly at neuromuscular junctionAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of protein metabolic processAmyloid-beta precursor proteinHomo sapiens (human)
neuron apoptotic processAmyloid-beta precursor proteinHomo sapiens (human)
smooth endoplasmic reticulum calcium ion homeostasisAmyloid-beta precursor proteinHomo sapiens (human)
neuron cellular homeostasisAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of ERK1 and ERK2 cascadeAmyloid-beta precursor proteinHomo sapiens (human)
response to interleukin-1Amyloid-beta precursor proteinHomo sapiens (human)
modulation of excitatory postsynaptic potentialAmyloid-beta precursor proteinHomo sapiens (human)
NMDA selective glutamate receptor signaling pathwayAmyloid-beta precursor proteinHomo sapiens (human)
regulation of spontaneous synaptic transmissionAmyloid-beta precursor proteinHomo sapiens (human)
cytosolic mRNA polyadenylationAmyloid-beta precursor proteinHomo sapiens (human)
negative regulation of long-term synaptic potentiationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of long-term synaptic potentiationAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of non-canonical NF-kappaB signal transductionAmyloid-beta precursor proteinHomo sapiens (human)
cellular response to amyloid-betaAmyloid-beta precursor proteinHomo sapiens (human)
regulation of presynapse assemblyAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of amyloid fibril formationAmyloid-beta precursor proteinHomo sapiens (human)
amyloid fibril formationAmyloid-beta precursor proteinHomo sapiens (human)
neuron projection maintenanceAmyloid-beta precursor proteinHomo sapiens (human)
positive regulation of T cell migrationAmyloid-beta precursor proteinHomo sapiens (human)
central nervous system developmentAmyloid-beta precursor proteinHomo sapiens (human)
kidney developmentNeprilysinHomo sapiens (human)
placenta developmentNeprilysinHomo sapiens (human)
proteolysisNeprilysinHomo sapiens (human)
peptide metabolic processNeprilysinHomo sapiens (human)
learning or memoryNeprilysinHomo sapiens (human)
substance P catabolic processNeprilysinHomo sapiens (human)
bradykinin catabolic processNeprilysinHomo sapiens (human)
sensory perception of painNeprilysinHomo sapiens (human)
protein catabolic processNeprilysinHomo sapiens (human)
lung developmentNeprilysinHomo sapiens (human)
hormone catabolic processNeprilysinHomo sapiens (human)
response to estrogenNeprilysinHomo sapiens (human)
creatinine metabolic processNeprilysinHomo sapiens (human)
amyloid-beta metabolic processNeprilysinHomo sapiens (human)
positive regulation of neurogenesisNeprilysinHomo sapiens (human)
neuropeptide processingNeprilysinHomo sapiens (human)
cellular response to cytokine stimulusNeprilysinHomo sapiens (human)
cellular response to UV-ANeprilysinHomo sapiens (human)
cellular response to UV-BNeprilysinHomo sapiens (human)
replicative senescenceNeprilysinHomo sapiens (human)
amyloid-beta clearanceNeprilysinHomo sapiens (human)
amyloid-beta clearance by cellular catabolic processNeprilysinHomo sapiens (human)
positive regulation of long-term synaptic potentiationNeprilysinHomo sapiens (human)
protein processingNeprilysinHomo sapiens (human)
response to hypoxiaAngiotensin-converting enzyme Homo sapiens (human)
kidney developmentAngiotensin-converting enzyme Homo sapiens (human)
blood vessel remodelingAngiotensin-converting enzyme Homo sapiens (human)
angiotensin maturationAngiotensin-converting enzyme Homo sapiens (human)
regulation of renal output by angiotensinAngiotensin-converting enzyme Homo sapiens (human)
neutrophil mediated immunityAngiotensin-converting enzyme Homo sapiens (human)
antigen processing and presentation of peptide antigen via MHC class IAngiotensin-converting enzyme Homo sapiens (human)
regulation of systemic arterial blood pressure by renin-angiotensinAngiotensin-converting enzyme Homo sapiens (human)
proteolysisAngiotensin-converting enzyme Homo sapiens (human)
spermatogenesisAngiotensin-converting enzyme Homo sapiens (human)
female pregnancyAngiotensin-converting enzyme Homo sapiens (human)
regulation of blood pressureAngiotensin-converting enzyme Homo sapiens (human)
male gonad developmentAngiotensin-converting enzyme Homo sapiens (human)
response to xenobiotic stimulusAngiotensin-converting enzyme Homo sapiens (human)
embryo development ending in birth or egg hatchingAngiotensin-converting enzyme Homo sapiens (human)
post-transcriptional regulation of gene expressionAngiotensin-converting enzyme Homo sapiens (human)
negative regulation of gene expressionAngiotensin-converting enzyme Homo sapiens (human)
substance P catabolic processAngiotensin-converting enzyme Homo sapiens (human)
bradykinin catabolic processAngiotensin-converting enzyme Homo sapiens (human)
regulation of smooth muscle cell migrationAngiotensin-converting enzyme Homo sapiens (human)
regulation of vasoconstrictionAngiotensin-converting enzyme Homo sapiens (human)
animal organ regenerationAngiotensin-converting enzyme Homo sapiens (human)
response to nutrient levelsAngiotensin-converting enzyme Homo sapiens (human)
response to lipopolysaccharideAngiotensin-converting enzyme Homo sapiens (human)
mononuclear cell proliferationAngiotensin-converting enzyme Homo sapiens (human)
response to laminar fluid shear stressAngiotensin-converting enzyme Homo sapiens (human)
angiotensin-activated signaling pathwayAngiotensin-converting enzyme Homo sapiens (human)
vasoconstrictionAngiotensin-converting enzyme Homo sapiens (human)
hormone metabolic processAngiotensin-converting enzyme Homo sapiens (human)
hormone catabolic processAngiotensin-converting enzyme Homo sapiens (human)
eating behaviorAngiotensin-converting enzyme Homo sapiens (human)
positive regulation of apoptotic processAngiotensin-converting enzyme Homo sapiens (human)
peptide catabolic processAngiotensin-converting enzyme Homo sapiens (human)
positive regulation of vasoconstrictionAngiotensin-converting enzyme Homo sapiens (human)
negative regulation of glucose importAngiotensin-converting enzyme Homo sapiens (human)
regulation of synaptic plasticityAngiotensin-converting enzyme Homo sapiens (human)
lung alveolus developmentAngiotensin-converting enzyme Homo sapiens (human)
amyloid-beta metabolic processAngiotensin-converting enzyme Homo sapiens (human)
arachidonic acid secretionAngiotensin-converting enzyme Homo sapiens (human)
positive regulation of neurogenesisAngiotensin-converting enzyme Homo sapiens (human)
heart contractionAngiotensin-converting enzyme Homo sapiens (human)
regulation of angiotensin metabolic processAngiotensin-converting enzyme Homo sapiens (human)
hematopoietic stem cell differentiationAngiotensin-converting enzyme Homo sapiens (human)
angiogenesis involved in coronary vascular morphogenesisAngiotensin-converting enzyme Homo sapiens (human)
cellular response to glucose stimulusAngiotensin-converting enzyme Homo sapiens (human)
response to dexamethasoneAngiotensin-converting enzyme Homo sapiens (human)
cell proliferation in bone marrowAngiotensin-converting enzyme Homo sapiens (human)
regulation of heart rate by cardiac conductionAngiotensin-converting enzyme Homo sapiens (human)
negative regulation of calcium ion importAngiotensin-converting enzyme Homo sapiens (human)
response to thyroid hormoneAngiotensin-converting enzyme Homo sapiens (human)
blood vessel diameter maintenanceAngiotensin-converting enzyme Homo sapiens (human)
regulation of hematopoietic stem cell proliferationAngiotensin-converting enzyme Homo sapiens (human)
negative regulation of gap junction assemblyAngiotensin-converting enzyme Homo sapiens (human)
cellular response to aldosteroneAngiotensin-converting enzyme Homo sapiens (human)
positive regulation of peptidyl-cysteine S-nitrosylationAngiotensin-converting enzyme Homo sapiens (human)
positive regulation of systemic arterial blood pressureAngiotensin-converting enzyme Homo sapiens (human)
regulation of cell growthType-1 angiotensin II receptorHomo sapiens (human)
kidney developmentType-1 angiotensin II receptorHomo sapiens (human)
renin-angiotensin regulation of aldosterone productionType-1 angiotensin II receptorHomo sapiens (human)
maintenance of blood vessel diameter homeostasis by renin-angiotensinType-1 angiotensin II receptorHomo sapiens (human)
regulation of systemic arterial blood pressure by renin-angiotensinType-1 angiotensin II receptorHomo sapiens (human)
G protein-coupled receptor signaling pathwayType-1 angiotensin II receptorHomo sapiens (human)
phospholipase C-activating G protein-coupled receptor signaling pathwayType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of cytosolic calcium ion concentrationType-1 angiotensin II receptorHomo sapiens (human)
Rho protein signal transductionType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of macrophage derived foam cell differentiationType-1 angiotensin II receptorHomo sapiens (human)
regulation of vasoconstrictionType-1 angiotensin II receptorHomo sapiens (human)
calcium-mediated signalingType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of phospholipase A2 activityType-1 angiotensin II receptorHomo sapiens (human)
low-density lipoprotein particle remodelingType-1 angiotensin II receptorHomo sapiens (human)
regulation of renal sodium excretionType-1 angiotensin II receptorHomo sapiens (human)
angiotensin-activated signaling pathwayType-1 angiotensin II receptorHomo sapiens (human)
regulation of cell population proliferationType-1 angiotensin II receptorHomo sapiens (human)
symbiont entry into host cellType-1 angiotensin II receptorHomo sapiens (human)
regulation of inflammatory responseType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of inflammatory responseType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of protein metabolic processType-1 angiotensin II receptorHomo sapiens (human)
cell chemotaxisType-1 angiotensin II receptorHomo sapiens (human)
phospholipase C-activating angiotensin-activated signaling pathwayType-1 angiotensin II receptorHomo sapiens (human)
blood vessel diameter maintenanceType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesisType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of CoA-transferase activityType-1 angiotensin II receptorHomo sapiens (human)
positive regulation of reactive oxygen species metabolic processType-1 angiotensin II receptorHomo sapiens (human)
inflammatory responseType-1 angiotensin II receptorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (37)

Processvia Protein(s)Taxonomy
RNA polymerase II cis-regulatory region sequence-specific DNA bindingAmyloid-beta precursor proteinHomo sapiens (human)
DNA bindingAmyloid-beta precursor proteinHomo sapiens (human)
serine-type endopeptidase inhibitor activityAmyloid-beta precursor proteinHomo sapiens (human)
signaling receptor bindingAmyloid-beta precursor proteinHomo sapiens (human)
protein bindingAmyloid-beta precursor proteinHomo sapiens (human)
heparin bindingAmyloid-beta precursor proteinHomo sapiens (human)
enzyme bindingAmyloid-beta precursor proteinHomo sapiens (human)
identical protein bindingAmyloid-beta precursor proteinHomo sapiens (human)
transition metal ion bindingAmyloid-beta precursor proteinHomo sapiens (human)
receptor ligand activityAmyloid-beta precursor proteinHomo sapiens (human)
PTB domain bindingAmyloid-beta precursor proteinHomo sapiens (human)
protein serine/threonine kinase bindingAmyloid-beta precursor proteinHomo sapiens (human)
signaling receptor activator activityAmyloid-beta precursor proteinHomo sapiens (human)
phosphatidylserine bindingNeprilysinHomo sapiens (human)
endopeptidase activityNeprilysinHomo sapiens (human)
metalloendopeptidase activityNeprilysinHomo sapiens (human)
protein bindingNeprilysinHomo sapiens (human)
exopeptidase activityNeprilysinHomo sapiens (human)
zinc ion bindingNeprilysinHomo sapiens (human)
peptide bindingNeprilysinHomo sapiens (human)
protein homodimerization activityNeprilysinHomo sapiens (human)
oligopeptidase activityNeprilysinHomo sapiens (human)
cardiolipin bindingNeprilysinHomo sapiens (human)
endopeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
carboxypeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
metalloendopeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
calmodulin bindingAngiotensin-converting enzyme Homo sapiens (human)
peptidase activityAngiotensin-converting enzyme Homo sapiens (human)
metallopeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
exopeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
tripeptidyl-peptidase activityAngiotensin-converting enzyme Homo sapiens (human)
peptidyl-dipeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
zinc ion bindingAngiotensin-converting enzyme Homo sapiens (human)
chloride ion bindingAngiotensin-converting enzyme Homo sapiens (human)
mitogen-activated protein kinase kinase bindingAngiotensin-converting enzyme Homo sapiens (human)
bradykinin receptor bindingAngiotensin-converting enzyme Homo sapiens (human)
mitogen-activated protein kinase bindingAngiotensin-converting enzyme Homo sapiens (human)
metallodipeptidase activityAngiotensin-converting enzyme Homo sapiens (human)
heterocyclic compound bindingAngiotensin-converting enzyme Homo sapiens (human)
angiotensin type I receptor activityType-1 angiotensin II receptorHomo sapiens (human)
angiotensin type II receptor activityType-1 angiotensin II receptorHomo sapiens (human)
protein bindingType-1 angiotensin II receptorHomo sapiens (human)
bradykinin receptor bindingType-1 angiotensin II receptorHomo sapiens (human)
protein heterodimerization activityType-1 angiotensin II receptorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (54)

Processvia Protein(s)Taxonomy
extracellular spaceAmyloid-beta precursor proteinHomo sapiens (human)
dendriteAmyloid-beta precursor proteinHomo sapiens (human)
extracellular regionAmyloid-beta precursor proteinHomo sapiens (human)
extracellular spaceAmyloid-beta precursor proteinHomo sapiens (human)
nuclear envelope lumenAmyloid-beta precursor proteinHomo sapiens (human)
cytoplasmAmyloid-beta precursor proteinHomo sapiens (human)
mitochondrial inner membraneAmyloid-beta precursor proteinHomo sapiens (human)
endosomeAmyloid-beta precursor proteinHomo sapiens (human)
early endosomeAmyloid-beta precursor proteinHomo sapiens (human)
endoplasmic reticulumAmyloid-beta precursor proteinHomo sapiens (human)
endoplasmic reticulum lumenAmyloid-beta precursor proteinHomo sapiens (human)
smooth endoplasmic reticulumAmyloid-beta precursor proteinHomo sapiens (human)
Golgi apparatusAmyloid-beta precursor proteinHomo sapiens (human)
Golgi lumenAmyloid-beta precursor proteinHomo sapiens (human)
Golgi-associated vesicleAmyloid-beta precursor proteinHomo sapiens (human)
cytosolAmyloid-beta precursor proteinHomo sapiens (human)
plasma membraneAmyloid-beta precursor proteinHomo sapiens (human)
clathrin-coated pitAmyloid-beta precursor proteinHomo sapiens (human)
cell-cell junctionAmyloid-beta precursor proteinHomo sapiens (human)
synaptic vesicleAmyloid-beta precursor proteinHomo sapiens (human)
cell surfaceAmyloid-beta precursor proteinHomo sapiens (human)
membraneAmyloid-beta precursor proteinHomo sapiens (human)
COPII-coated ER to Golgi transport vesicleAmyloid-beta precursor proteinHomo sapiens (human)
axonAmyloid-beta precursor proteinHomo sapiens (human)
growth coneAmyloid-beta precursor proteinHomo sapiens (human)
platelet alpha granule lumenAmyloid-beta precursor proteinHomo sapiens (human)
neuromuscular junctionAmyloid-beta precursor proteinHomo sapiens (human)
endosome lumenAmyloid-beta precursor proteinHomo sapiens (human)
trans-Golgi network membraneAmyloid-beta precursor proteinHomo sapiens (human)
ciliary rootletAmyloid-beta precursor proteinHomo sapiens (human)
dendritic spineAmyloid-beta precursor proteinHomo sapiens (human)
dendritic shaftAmyloid-beta precursor proteinHomo sapiens (human)
perikaryonAmyloid-beta precursor proteinHomo sapiens (human)
membrane raftAmyloid-beta precursor proteinHomo sapiens (human)
apical part of cellAmyloid-beta precursor proteinHomo sapiens (human)
synapseAmyloid-beta precursor proteinHomo sapiens (human)
perinuclear region of cytoplasmAmyloid-beta precursor proteinHomo sapiens (human)
presynaptic active zoneAmyloid-beta precursor proteinHomo sapiens (human)
spindle midzoneAmyloid-beta precursor proteinHomo sapiens (human)
recycling endosomeAmyloid-beta precursor proteinHomo sapiens (human)
extracellular exosomeAmyloid-beta precursor proteinHomo sapiens (human)
receptor complexAmyloid-beta precursor proteinHomo sapiens (human)
early endosomeAmyloid-beta precursor proteinHomo sapiens (human)
membrane raftAmyloid-beta precursor proteinHomo sapiens (human)
cell surfaceAmyloid-beta precursor proteinHomo sapiens (human)
Golgi apparatusAmyloid-beta precursor proteinHomo sapiens (human)
plasma membraneAmyloid-beta precursor proteinHomo sapiens (human)
cytoplasmNeprilysinHomo sapiens (human)
early endosomeNeprilysinHomo sapiens (human)
trans-Golgi networkNeprilysinHomo sapiens (human)
plasma membraneNeprilysinHomo sapiens (human)
brush borderNeprilysinHomo sapiens (human)
focal adhesionNeprilysinHomo sapiens (human)
synaptic vesicleNeprilysinHomo sapiens (human)
cell surfaceNeprilysinHomo sapiens (human)
membraneNeprilysinHomo sapiens (human)
axonNeprilysinHomo sapiens (human)
dendriteNeprilysinHomo sapiens (human)
secretory granule membraneNeprilysinHomo sapiens (human)
cytoplasmic vesicleNeprilysinHomo sapiens (human)
neuronal cell bodyNeprilysinHomo sapiens (human)
neuron projection terminusNeprilysinHomo sapiens (human)
membrane raftNeprilysinHomo sapiens (human)
synapseNeprilysinHomo sapiens (human)
extracellular exosomeNeprilysinHomo sapiens (human)
presynapseNeprilysinHomo sapiens (human)
plasma membraneNeprilysinHomo sapiens (human)
extracellular spaceAngiotensin-converting enzyme Homo sapiens (human)
extracellular regionAngiotensin-converting enzyme Homo sapiens (human)
extracellular spaceAngiotensin-converting enzyme Homo sapiens (human)
lysosomeAngiotensin-converting enzyme Homo sapiens (human)
endosomeAngiotensin-converting enzyme Homo sapiens (human)
plasma membraneAngiotensin-converting enzyme Homo sapiens (human)
external side of plasma membraneAngiotensin-converting enzyme Homo sapiens (human)
basal plasma membraneAngiotensin-converting enzyme Homo sapiens (human)
brush border membraneAngiotensin-converting enzyme Homo sapiens (human)
extracellular exosomeAngiotensin-converting enzyme Homo sapiens (human)
sperm midpieceAngiotensin-converting enzyme Homo sapiens (human)
plasma membraneAngiotensin-converting enzyme Homo sapiens (human)
plasma membraneType-1 angiotensin II receptorHomo sapiens (human)
membraneType-1 angiotensin II receptorHomo sapiens (human)
plasma membraneType-1 angiotensin II receptorHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (46)

Assay IDTitleYearJournalArticle
AID1676592Binding affinity to Gallium ion assessed as performance ratio ratio by measuring product of accounting ratio and retention ratio at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1676591Binding affinity to Nickel cation assessed as accounting ratio by measuring total compound detected/total compound adsorbed at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1515584Inhibition of APP (unknown origin)
AID383259Antihypertensive effect in anesthetized Wistar rat2008European journal of medicinal chemistry, Mar, Volume: 43, Issue:3
Synthesis and antihypertensive effects of new methylthiomorpholinphenol derivatives.
AID37663In vitro inhibitory activity against Angiotensin I converting enzyme (ACE) isolated from rabbit lung extract using hippuryl-L-histidyl-L-leucine (HHL) as the substrate1999Journal of medicinal chemistry, Jan-28, Volume: 42, Issue:2
Vasopeptidase inhibitors: incorporation of geminal and spirocyclic substituted azepinones in mercaptoacyl dipeptides.
AID1515582Displacement of Europium-labeled angiotensin-2 from human AT2 receptor expressed in CHOK1 cell membranes after 120 mins by DELFIA
AID1676589Binding affinity to Nickel cation assessed as performance ratio ratio by measuring product of accounting ratio and retention ratio at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1515581Inhibition of NEP (unknown origin) preincubated for 10 mins followed by fluorogenic substrate addition and measured after 20 mins by fluorescence assay
AID37645In vitro inhibition of ACE (Angiotensin I converting enzyme) isolated from rabbit lung extract1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1676600Binding affinity to zinc ion assessed as accounting ratio by measuring total compound detected/total compound adsorbed at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1515578Displacement of Europium-labeled angiotensin-2 from human AT1 receptor expressed in CHOK1 cell membranes after 120 mins by DELFIA
AID147231In vitro inhibition of neutral endopeptidase purified from rat kidney using fluorimetry assay1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1676602Binding affinity to ferric ion assessed as accounting ratio by measuring total compound detected/total compound adsorbed at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1423288Inhibition of human fully glycosylated ACE C-terminal domain expressed in CHO cells using Cbz-Phe-His-Leu as substrate preincubated for 15 mins followed by substrate addition measured after 10 mins by Morrison's plot analysis2018Journal of medicinal chemistry, 11-21, Volume: 61, Issue:22
Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design.
AID1607322Inhibition of rat kidney NEP using dansyl-Gly-Phe-Arg as substrate by fluorometric assay2020Journal of medicinal chemistry, 05-28, Volume: 63, Issue:10
Molecular Basis for Omapatrilat and Sampatrilat Binding to Neprilysin-Implications for Dual Inhibitor Design with Angiotensin-Converting Enzyme.
AID147361In vitro inhibitory activity against purified rat kidney neutral endopeptidase (NEP) using a fluorometric assay with dansyl-Gly-Phe-Arg as the substrate1999Journal of medicinal chemistry, Jan-28, Volume: 42, Issue:2
Vasopeptidase inhibitors: incorporation of geminal and spirocyclic substituted azepinones in mercaptoacyl dipeptides.
AID1423284Inhibition of human fully glycosylated ACE C-terminal domain expressed in CHO cells using Cbz-Phe-His-Leu as substrate preincubated for 15 mins followed by substrate addition measured after 10 mins by fluorescence spectrophotometric analysis2018Journal of medicinal chemistry, 11-21, Volume: 61, Issue:22
Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design.
AID1676598Binding affinity to cupric ion assessed as retention ratio by measuring compound detected in elution fraction/total compound detected at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1676601Binding affinity to Zinc ion assessed as retention ratio by measuring compound detected in elution fraction/total compound detected at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1515586Antihypertensive activity in spontaneously hypertensive rat assessed as reduction in mean arterial pressure administered via oral gavage in ascending cumulative doses every 60 mins measured up to 24 hrs by telemetry method
AID1676595Binding affinity to Ferric ion assessed as performance ratio ratio by measuring product of accounting ratio and retention ratio at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1676596Binding affinity to Ferric ion assessed as retention ratio by measuring compound detected in elution fraction/total compound detected at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID444546Inhibition of human somatic ACE C-terminal domain2010Journal of medicinal chemistry, Jan-14, Volume: 53, Issue:1
Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors.
AID1515588Antihypertensive activity in DOCA salt-induced CD-1 rat model of hypertension assessed as reduction in blood pressure administered via oral gavage in ascending cumulative doses every 60 mins measured up to 24 hrs by telemetry method
AID1515592Induction of angioedema in normotensive rat assessed as increase in tracheal plasma extravasation by measuring Evans blue dye leakage into peritracheal tissue at 0.3 to 3 mg/kg, po
AID182477% inhibition of AI pressor response at 60 minutes after intravenous administration of 0.5 micro mol/kg of compound in rat1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1515585Inhibition of recombinant human ECE1
AID37787Inhibition of Angiotensin I converting enzyme2000Bioorganic & medicinal chemistry letters, Feb-07, Volume: 10, Issue:3
N-formyl hydroxylamine containing dipeptides: generation of a new class of vasopeptidase inhibitors.
AID147368Inhibition of Neutral endopeptidase2000Bioorganic & medicinal chemistry letters, Feb-07, Volume: 10, Issue:3
N-formyl hydroxylamine containing dipeptides: generation of a new class of vasopeptidase inhibitors.
AID17740050% inhibition of the AI pressor response in normotensive rat after intravenous administration at a dose 0.5 umol/kg1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1423287Inhibition of human fully glycosylated ACE N-terminal domain expressed in CHO cells using Cbz-Phe-His-Leu as substrate preincubated for 15 mins followed by substrate addition measured after 10 mins by Morrison's plot analysis2018Journal of medicinal chemistry, 11-21, Volume: 61, Issue:22
Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design.
AID1676597Binding affinity to cupric ion assessed as performance ratio ratio by measuring product of accounting ratio and retention ratio at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID1676588Binding affinity to Zinc ion assessed as performance ratio ratio by measuring product of accounting ratio and retention ratio at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID182342% inhibition of AI pressor response at 30 minutes after intravenous administration of 0.5 micro mol/kg of compound in rat1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID182339% inhibition of AI pressor response at 120 minutes after intravenous administration of 0.5 micro mol/kg of compound in rat1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1676594Binding affinity to gallium ion assessed as accounting ratio by measuring total compound detected/total compound adsorbed at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID444547Inhibition of human somatic NEP2010Journal of medicinal chemistry, Jan-14, Volume: 53, Issue:1
Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors.
AID1515580In vivo inhibition of NEP in Sprague-Dawley rat assessed as potentiation of ANP-induced elevation of urinary cGMP level at 3 mg/kg, iv treated for 5 mins at 15 mins post 2 doses of angiotensin-2 treatment at 15 minutes apart followed by ANP treatment meas
AID1676590Binding affinity to Nickel cation assessed as retention ratio by measuring compound detected in elution fraction/total compound detected at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID186841Decreased Mean arterial pressure (MAP) in rat after single oral dose of 30 umol/kg1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1676599Binding affinity to cupric ion assessed as accounting ratio by measuring total compound detected/total compound adsorbed at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID176497Compound is evaluated for the dose required for 50% inhibition of AI pressor response in normotensive rats1999Journal of medicinal chemistry, Jan-28, Volume: 42, Issue:2
Vasopeptidase inhibitors: incorporation of geminal and spirocyclic substituted azepinones in mercaptoacyl dipeptides.
AID1515583Inhibition of recombinant human ACE using Mca-BK2 as substrate preincubated for 10 mins followed by fluorogenic substrate addition and measured after 20 mins by fluorescence assay
AID1676593Binding affinity to Gallium ion assessed as retention ratio by measuring compound detected in elution fraction/total compound detected at 2.55 umol by immobilized metal-ion affinity chromatography2020Journal of medicinal chemistry, 10-22, Volume: 63, Issue:20
Immobilized Metal Affinity Chromatography as a Drug Discovery Platform for Metalloenzyme Inhibitors.
AID182341% inhibition of AI pressor response at 2 minutes after intravenous administration of 0.5 micro mol/kg of compound in rat1997Journal of medicinal chemistry, May-23, Volume: 40, Issue:11
Dual metalloprotease inhibitors: mercaptoacetyl-based fused heterocyclic dipeptide mimetics as inhibitors of angiotensin-converting enzyme and neutral endopeptidase.
AID1423283Inhibition of human fully glycosylated ACE N-terminal domain expressed in CHO cells using Cbz-Phe-His-Leu as substrate preincubated for 15 mins followed by substrate addition measured after 10 mins by fluorescence spectrophotometric analysis2018Journal of medicinal chemistry, 11-21, Volume: 61, Issue:22
Molecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (215)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's16 (7.44)18.2507
2000's174 (80.93)29.6817
2010's20 (9.30)24.3611
2020's5 (2.33)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 42.18

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be strong demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index42.18 (24.57)
Research Supply Index5.56 (2.92)
Research Growth Index4.86 (4.65)
Search Engine Demand Index65.76 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (42.18)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials33 (14.60%)5.53%
Reviews48 (21.24%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other145 (64.16%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]