Page last updated: 2024-12-08

jtp 4819

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth

Description

JTP 4819: a prolyl endopeptidase inhibitor; structure given in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID178060
CHEMBL ID76578
SCHEMBL ID194809
MeSH IDM0248245

Synonyms (21)

Synonym
CHEMBL76578 ,
(s)-n-benzyl-2-((s)-2-(2-hydroxyacetyl)pyrrolidine-1-carbonyl)pyrrolidine-1-carboxamide
(s)-2-[(s)-2-(2-hydroxy-acetyl)-pyrrolidine-1-carbonyl]-pyrrolidine-1-carboxylic acid benzylamide
bdbm50051495
jtp-4819
jtp 4819
(2s)-n-benzyl-2-[(2s)-2-(2-hydroxyacetyl)pyrrolidine-1-carbonyl]pyrrolidine-1-carboxamide
unii-asg803l8rd
asg803l8rd ,
162203-65-8
1-pyrrolidinecarboxamide, 2-(((2s)-2-(hydroxyacetyl)-1-pyrrolidinyl)carbonyl)-n-(phenylmethyl)-, (2s)-
2-((2-(hydroxyacetyl)-1-pyrrolidinyl)carbonyl)-n-(phenylmethyl)-1-pyrrolidinecarboxamide
SCHEMBL194809
ICULFJDHZQTNRB-HOTGVXAUSA-N ,
(s)-2-[[(s)-2-(hydroxyacetyl)-1-pyrrolidinyl]carbonyl]-n-(phenylmethyl)-1-pyrrolidinecarboxamide
n-benzyl-2-[2-(hydroxyacetyl)pyrrolidine-1-carbonyl]pyrrolidine-1-carboximidic acid
DTXSID40936657
2-(2-(2-hydroxy-acetyl)-pyrrolidine-1-carbonyl-pyrrolidine-1-carboxylic acid benzylamide, 2s-, l-
1-pyrrolidinecarboxamide, 2-((2-(hydroxyacetyl)-1-pyrrolidinyl)carbonyl)-n-(phenylmethyl)-, (s-(r*,r*))-
(2s)-2-(((2s)-2-(hydroxyacetyl)-1-pyrrolidinyl)carbonyl)-n-(phenylmethyl)-1-pyrrolidinecarboxamide
1-pyrrolidinecarboxamide, 2-[[(2s)-2-(hydroxyacetyl)-1-pyrrolidinyl]carbonyl]-n-(phenylmethyl)-, (2s)-

Research Excerpts

Toxicity

ExcerptReferenceRelevance
"These results indicate that JTP-4819 has acceptable pharmacodynamic and pharmacokinetics profiles for clinical use without any serious adverse events as we verified in healthy young male volunteers."( Pharmacokinetics and safety of JTP-4819, a novel specific orally active prolyl endopeptidase inhibitor, in healthy male volunteers.
Ikeda, Y; Kobayashi, T; Kondo, K; Nakashima, M; Umemura, K; Urata, Y, 1997
)
0.3

Pharmacokinetics

ExcerptReferenceRelevance
"These results indicate that JTP-4819 has acceptable pharmacodynamic and pharmacokinetics profiles for clinical use without any serious adverse events as we verified in healthy young male volunteers."( Pharmacokinetics and safety of JTP-4819, a novel specific orally active prolyl endopeptidase inhibitor, in healthy male volunteers.
Ikeda, Y; Kobayashi, T; Kondo, K; Nakashima, M; Umemura, K; Urata, Y, 1997
)
0.3

Bioavailability

ExcerptReferenceRelevance
" With the single dose of 60 mg, a cross-over study was conducted to examine the effect of food on the bioavailability of the drug."( Pharmacokinetics and safety of JTP-4819, a novel specific orally active prolyl endopeptidase inhibitor, in healthy male volunteers.
Ikeda, Y; Kobayashi, T; Kondo, K; Nakashima, M; Umemura, K; Urata, Y, 1997
)
0.3
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (6)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Prolyl endopeptidaseRattus norvegicus (Norway rat)IC50 (µMol)0.00010.00010.12430.3000AID161121
Xaa-Pro dipeptidaseHomo sapiens (human)IC50 (µMol)100.00004.90004.90004.9000AID481405
Prolyl endopeptidaseSus scrofa (pig)IC50 (µMol)0.00020.00020.01050.1300AID242814; AID282686
Prolyl endopeptidaseSus scrofa (pig)Ki0.00010.00000.00010.0001AID1307742
Dipeptidyl peptidase 4Homo sapiens (human)IC50 (µMol)100.00000.00010.444410.0000AID481403
Cytosol aminopeptidaseHomo sapiens (human)IC50 (µMol)100.00000.30000.30000.3000AID481413
Lysosomal Pro-X carboxypeptidaseHomo sapiens (human)IC50 (µMol)100.00000.00530.60331.9000AID481406
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (31)

Processvia Protein(s)Taxonomy
proteolysisXaa-Pro dipeptidaseHomo sapiens (human)
amino acid metabolic processXaa-Pro dipeptidaseHomo sapiens (human)
collagen catabolic processXaa-Pro dipeptidaseHomo sapiens (human)
negative regulation of programmed cell deathXaa-Pro dipeptidaseHomo sapiens (human)
behavioral fear responseDipeptidyl peptidase 4Homo sapiens (human)
response to hypoxiaDipeptidyl peptidase 4Homo sapiens (human)
proteolysisDipeptidyl peptidase 4Homo sapiens (human)
cell adhesionDipeptidyl peptidase 4Homo sapiens (human)
positive regulation of cell population proliferationDipeptidyl peptidase 4Homo sapiens (human)
negative regulation of extracellular matrix disassemblyDipeptidyl peptidase 4Homo sapiens (human)
peptide hormone processingDipeptidyl peptidase 4Homo sapiens (human)
receptor-mediated endocytosis of virus by host cellDipeptidyl peptidase 4Homo sapiens (human)
T cell costimulationDipeptidyl peptidase 4Homo sapiens (human)
regulation of cell-cell adhesion mediated by integrinDipeptidyl peptidase 4Homo sapiens (human)
locomotory exploration behaviorDipeptidyl peptidase 4Homo sapiens (human)
psychomotor behaviorDipeptidyl peptidase 4Homo sapiens (human)
T cell activationDipeptidyl peptidase 4Homo sapiens (human)
endothelial cell migrationDipeptidyl peptidase 4Homo sapiens (human)
symbiont entry into host cellDipeptidyl peptidase 4Homo sapiens (human)
receptor-mediated virion attachment to host cellDipeptidyl peptidase 4Homo sapiens (human)
negative chemotaxisDipeptidyl peptidase 4Homo sapiens (human)
membrane fusionDipeptidyl peptidase 4Homo sapiens (human)
negative regulation of neutrophil chemotaxisDipeptidyl peptidase 4Homo sapiens (human)
glucagon processingDipeptidyl peptidase 4Homo sapiens (human)
proteolysisCytosol aminopeptidaseHomo sapiens (human)
regulation of thyroid hormone mediated signaling pathwayLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
plasma kallikrein-kinin cascadeLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
proteolysisLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
glucose homeostasisLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
energy homeostasisLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
regulation of reactive oxygen species metabolic processLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
angiogenesis involved in wound healingLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
negative regulation of systemic arterial blood pressureLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
regulation of blood vessel endothelial cell migrationLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (19)

Processvia Protein(s)Taxonomy
metallocarboxypeptidase activityXaa-Pro dipeptidaseHomo sapiens (human)
protein bindingXaa-Pro dipeptidaseHomo sapiens (human)
manganese ion bindingXaa-Pro dipeptidaseHomo sapiens (human)
metalloaminopeptidase activityXaa-Pro dipeptidaseHomo sapiens (human)
proline dipeptidase activityXaa-Pro dipeptidaseHomo sapiens (human)
peptidase activityXaa-Pro dipeptidaseHomo sapiens (human)
virus receptor activityDipeptidyl peptidase 4Homo sapiens (human)
protease bindingDipeptidyl peptidase 4Homo sapiens (human)
aminopeptidase activityDipeptidyl peptidase 4Homo sapiens (human)
serine-type endopeptidase activityDipeptidyl peptidase 4Homo sapiens (human)
signaling receptor bindingDipeptidyl peptidase 4Homo sapiens (human)
protein bindingDipeptidyl peptidase 4Homo sapiens (human)
serine-type peptidase activityDipeptidyl peptidase 4Homo sapiens (human)
dipeptidyl-peptidase activityDipeptidyl peptidase 4Homo sapiens (human)
identical protein bindingDipeptidyl peptidase 4Homo sapiens (human)
protein homodimerization activityDipeptidyl peptidase 4Homo sapiens (human)
chemorepellent activityDipeptidyl peptidase 4Homo sapiens (human)
aminopeptidase activityCytosol aminopeptidaseHomo sapiens (human)
carboxypeptidase activityCytosol aminopeptidaseHomo sapiens (human)
protein bindingCytosol aminopeptidaseHomo sapiens (human)
metalloexopeptidase activityCytosol aminopeptidaseHomo sapiens (human)
manganese ion bindingCytosol aminopeptidaseHomo sapiens (human)
metalloaminopeptidase activityCytosol aminopeptidaseHomo sapiens (human)
peptidase activityCytosol aminopeptidaseHomo sapiens (human)
serine-type carboxypeptidase activityLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
protein bindingLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
dipeptidyl-peptidase activityLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (20)

Processvia Protein(s)Taxonomy
extracellular exosomeXaa-Pro dipeptidaseHomo sapiens (human)
extracellular regionDipeptidyl peptidase 4Homo sapiens (human)
lysosomal membraneDipeptidyl peptidase 4Homo sapiens (human)
plasma membraneDipeptidyl peptidase 4Homo sapiens (human)
focal adhesionDipeptidyl peptidase 4Homo sapiens (human)
cell surfaceDipeptidyl peptidase 4Homo sapiens (human)
membraneDipeptidyl peptidase 4Homo sapiens (human)
apical plasma membraneDipeptidyl peptidase 4Homo sapiens (human)
lamellipodiumDipeptidyl peptidase 4Homo sapiens (human)
endocytic vesicleDipeptidyl peptidase 4Homo sapiens (human)
lamellipodium membraneDipeptidyl peptidase 4Homo sapiens (human)
membrane raftDipeptidyl peptidase 4Homo sapiens (human)
intercellular canaliculusDipeptidyl peptidase 4Homo sapiens (human)
extracellular exosomeDipeptidyl peptidase 4Homo sapiens (human)
plasma membraneDipeptidyl peptidase 4Homo sapiens (human)
nucleusCytosol aminopeptidaseHomo sapiens (human)
trans-Golgi networkCytosol aminopeptidaseHomo sapiens (human)
focal adhesionCytosol aminopeptidaseHomo sapiens (human)
extracellular exosomeCytosol aminopeptidaseHomo sapiens (human)
cytoplasmCytosol aminopeptidaseHomo sapiens (human)
plasma membraneLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
azurophil granule membraneLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
intracellular membrane-bounded organelleLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
basal part of cellLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
extracellular exosomeLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
ficolin-1-rich granule membraneLysosomal Pro-X carboxypeptidaseHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (14)

Assay IDTitleYearJournalArticle
AID241048Inhibitory activity against prolyl oligopeptidase of porcine brain homogenate2004Journal of medicinal chemistry, Nov-04, Volume: 47, Issue:23
A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors.
AID481392Inhibition of POP in rat brain homogenate2010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
AID481404Inhibition of APP2010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
AID1307742Inhibition of poricne brain POP in expressed in Escherichia coli TOP10 competent cells pre-incubated for 2 hrs before Z-Gly-Pro-AMC substrate addition and monitored every 1 min for 30 mins2016Journal of medicinal chemistry, 05-12, Volume: 59, Issue:9
3-Oxo-hexahydro-1H-isoindole-4-carboxylic Acid as a Drug Chiral Bicyclic Scaffold: Structure-Based Design and Preparation of Conformationally Constrained Covalent and Noncovalent Prolyl Oligopeptidase Inhibitors.
AID237428Partition coefficient (logP) determined in a 1-octanol-phosphate buffer system2004Journal of medicinal chemistry, Nov-04, Volume: 47, Issue:23
A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors.
AID481413Inhibition of proline iminopeptidase)2010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
AID1896133Inhibition of POP (unknown origin)2022European journal of medicinal chemistry, Oct-05, Volume: 240Modulating the selectivity of inhibitors for prolyl oligopeptidase inhibitors and fibroblast activation protein-α for different indications.
AID481403Inhibition of DPP42010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
AID161121Inhibitory activity was evaluated against Post-proline cleaving enzyme from rat brain1996Journal of medicinal chemistry, Jun-07, Volume: 39, Issue:12
New prolyl endopeptidase inhibitors: in vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1]heptane, and perhydroindole derivatives.
AID242814In vitro inhibitory activity against porcine prolyl oligopeptidase by using 4 mM Suc-Gly-Pro-7-amido-4-methylcoumarin as substrate (pH 7.0) at 30 degree C for 60 min2005Journal of medicinal chemistry, Jul-28, Volume: 48, Issue:15
Dicarboxylic acid azacycle l-prolyl-pyrrolidine amides as prolyl oligopeptidase inhibitors and three-dimensional quantitative structure-activity relationship of the enzyme-inhibitor interactions.
AID282686Inhibition of pig brain POP2005Journal of medicinal chemistry, Nov-17, Volume: 48, Issue:23
Synthesis and characterization of the novel fluorescent prolyl oligopeptidase inhibitor 4-fluoresceinthiocarbamoyl-6-aminocaproyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine.
AID481405Inhibition of prolidase2010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
AID238565Inhibitory activity against prolyl oligopeptidase of porcine brain homogenate2004Journal of medicinal chemistry, Nov-04, Volume: 47, Issue:23
A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors.
AID481406Inhibition of carboxypeptidase P2010Journal of medicinal chemistry, May-13, Volume: 53, Issue:9
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (25)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's13 (52.00)18.2507
2000's6 (24.00)29.6817
2010's5 (20.00)24.3611
2020's1 (4.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials1 (4.00%)5.53%
Reviews2 (8.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other22 (88.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]