Compounds > cyclotheonamide a
Page last updated: 2024-12-10

cyclotheonamide a

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

Description

cyclotheonamide A: a cyclic peptide isolated from the marine sponge Theonella; structure given in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID5287991
CHEMBL ID342672
SCHEMBL ID1230642
MeSH IDM0218583

Synonyms (18)

Synonym
3-((4-amino-5-(4-hydroxyphenyl)-1-oxo-2-pentenyl)amino)-n-formyl-l-alanyl-d-prolyl-6-((aminoiminomethyl)amino)-2-oxo-3-aminohexanoyl-l-phenylalanine cyclic (4-1)-peptide
l-phenylalanine, 3-((4-amino-5-(4-hydroxyphenyl)-1-oxo-2-pentenyl)amino)-n-formyl-l-alanyl-d-prolyl-6-((aminoiminomethyl)amino)-2-oxo-3-aminohexanoyl-, cyclic (4-1)-peptide
unii-2y1teh8ew7
2y1teh8ew7 ,
DB04269
cyclotheonamide a
CHEMBL342672 ,
bdbm50118723
n-[(3s,7e,9s,12r,16s,19s)-12-benzyl-16-[3-(diaminomethylideneamino)propyl]-9-[(4-hydroxyphenyl)methyl]-2,6,11,14,15,18-hexaoxo-1,5,10,13,17-pentazabicyclo[17.3.0]docos-7-en-3-yl]formamide
cyclotheonamide a [mi]
ms-1144
cyclo((2s)-2-(formylamino)-.beta.-alanyl-l-prolyl-(3s)-3-amino-6-((aminoiminomethyl)amino)-2-oxohexanoyl-d-phenylalanyl-(2e,4s)-4-amino-5-(4-hydroxyphenyl)-2-pentenoyl)
SCHEMBL1230642
1-{3-[(3s,7r,10s,11e,16s,21as)-7-benzyl-16-(formylamino)-10-(4-hydroxybenzyl)-1,4,5,8,13,17-hexaoxo-2,3,4,5,6,7,8,9,10,13,14,15,16,17,19,20,21,21a-octadecahydro-1h-pyrrolo[2,1-j][1,4,8,11,15]pentaazacyclononadecin-3-yl]propyl}guanidine
Q27095088
n-((3s,7r,10s,16s,21as,e)-7-benzyl-3-(3-guanidinopropyl)-10-(4-hydroxybenzyl)-1,4,5,8,13,17-hexaoxo-2,3,4,5,6,7,8,9,10,13,14,15,16,17,19,20,21,21a-octadecahydro-1h-pyrrolo[2,1-j][1,4,8,11,15]pentaazacyclononadecin-16-yl)formamide
CS-0079260
HY-120822

Research Excerpts

Bioavailability

ExcerptReferenceRelevance
" The bioavailability in rats and dogs could be drastically altered depending on the overall charge distribution in the molecule."( Unique overlap in the prerequisites for thrombin inhibition and oral bioavailability resulting in potent oral antithrombotics.
Adang, AE; de Man, AP; Grootenhuis, PD; Kelder, J; Lucas, H; Meuleman, DG; Peters, CA; Rewinkel, JB; Smit, MJ; van Aelst, S; van Boeckel, CA; van Dinther, T; Visser, A; Vogel, GM, 2002)		0.31
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (1)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
ProthrombinHomo sapiens (human)IC50 (µMol)0.76150.00000.710710.0000AID401046; AID539764
ProthrombinHomo sapiens (human)Ki0.09050.00000.78469.0000AID211014; AID711506
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (33)

Processvia Protein(s)Taxonomy
positive regulation of protein phosphorylationProthrombinHomo sapiens (human)
proteolysisProthrombinHomo sapiens (human)
acute-phase responseProthrombinHomo sapiens (human)
cell surface receptor signaling pathwayProthrombinHomo sapiens (human)
G protein-coupled receptor signaling pathwayProthrombinHomo sapiens (human)
blood coagulationProthrombinHomo sapiens (human)
positive regulation of cell population proliferationProthrombinHomo sapiens (human)
regulation of cell shapeProthrombinHomo sapiens (human)
response to woundingProthrombinHomo sapiens (human)
negative regulation of platelet activationProthrombinHomo sapiens (human)
platelet activationProthrombinHomo sapiens (human)
regulation of blood coagulationProthrombinHomo sapiens (human)
positive regulation of blood coagulationProthrombinHomo sapiens (human)
positive regulation of cell growthProthrombinHomo sapiens (human)
positive regulation of insulin secretionProthrombinHomo sapiens (human)
positive regulation of collagen biosynthetic processProthrombinHomo sapiens (human)
fibrinolysisProthrombinHomo sapiens (human)
negative regulation of proteolysisProthrombinHomo sapiens (human)
positive regulation of receptor signaling pathway via JAK-STATProthrombinHomo sapiens (human)
negative regulation of astrocyte differentiationProthrombinHomo sapiens (human)
positive regulation of release of sequestered calcium ion into cytosolProthrombinHomo sapiens (human)
regulation of cytosolic calcium ion concentrationProthrombinHomo sapiens (human)
cytolysis by host of symbiont cellsProthrombinHomo sapiens (human)
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductionProthrombinHomo sapiens (human)
negative regulation of fibrinolysisProthrombinHomo sapiens (human)
antimicrobial humoral immune response mediated by antimicrobial peptideProthrombinHomo sapiens (human)
neutrophil-mediated killing of gram-negative bacteriumProthrombinHomo sapiens (human)
positive regulation of lipid kinase activityProthrombinHomo sapiens (human)
negative regulation of cytokine production involved in inflammatory responseProthrombinHomo sapiens (human)
positive regulation of protein localization to nucleusProthrombinHomo sapiens (human)
positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathwayProthrombinHomo sapiens (human)
ligand-gated ion channel signaling pathwayProthrombinHomo sapiens (human)
positive regulation of reactive oxygen species metabolic processProthrombinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (8)

Processvia Protein(s)Taxonomy
lipopolysaccharide bindingProthrombinHomo sapiens (human)
serine-type endopeptidase activityProthrombinHomo sapiens (human)
signaling receptor bindingProthrombinHomo sapiens (human)
calcium ion bindingProthrombinHomo sapiens (human)
protein bindingProthrombinHomo sapiens (human)
growth factor activityProthrombinHomo sapiens (human)
heparin bindingProthrombinHomo sapiens (human)
thrombospondin receptor activityProthrombinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (9)

Processvia Protein(s)Taxonomy
external side of plasma membraneProthrombinHomo sapiens (human)
collagen-containing extracellular matrixProthrombinHomo sapiens (human)
extracellular regionProthrombinHomo sapiens (human)
extracellular spaceProthrombinHomo sapiens (human)
endoplasmic reticulum lumenProthrombinHomo sapiens (human)
Golgi lumenProthrombinHomo sapiens (human)
plasma membraneProthrombinHomo sapiens (human)
extracellular exosomeProthrombinHomo sapiens (human)
blood microparticleProthrombinHomo sapiens (human)
collagen-containing extracellular matrixProthrombinHomo sapiens (human)
extracellular spaceProthrombinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (5)

Assay IDTitleYearJournalArticle
AID539764Inhibition of factor 2a2010Bioorganic & medicinal chemistry letters, Dec-01, Volume: 20, Issue:23
Design and synthesis of macrocyclic indoles targeting blood coagulation cascade Factor XIa.
AID401047Inhibition of trypsin1998Journal of natural products, May, Volume: 61, Issue:5
Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella.
AID711506Inhibition of thrombin2011Journal of medicinal chemistry, Apr-14, Volume: 54, Issue:7
Macrocycles are great cycles: applications, opportunities, and challenges of synthetic macrocycles in drug discovery.
AID211014Inhibitory activity against thrombin.2002Journal of medicinal chemistry, Sep-26, Volume: 45, Issue:20
Unique overlap in the prerequisites for thrombin inhibition and oral bioavailability resulting in potent oral antithrombotics.
AID401046Inhibition of thrombin1998Journal of natural products, May, Volume: 61, Issue:5
Cyclotheonamides E2 and E3, new potent serine protease inhibitors from the marine sponge of the genus Theonella.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (10)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's5 (50.00)18.2507
2000's2 (20.00)29.6817
2010's3 (30.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 11.86

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 weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index11.86 (24.57)
Research Supply Index2.40 (2.92)
Research Growth Index4.25 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (11.86)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews1 (10.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other9 (90.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
mci 9038
[no description available]		2.0110peptide
melagatran
[no description available]		2.0110azetidines;
carboxamidine;
dicarboxylic acid monoamide;
non-proteinogenic alpha-amino acid;
secondary amino compound		anticoagulant;
EC 3.4.21.5 (thrombin) inhibitor;
serine protease inhibitor
darunavir
Darunavir: An HIV PROTEASE INHIBITOR that is used in the treatment of AIDS and HIV INFECTIONS. Due to the emergence of ANTIVIRAL DRUG RESISTANCE when used alone, it is administered in combination with other ANTI-HIV AGENTS.. darunavir : An N,N-disubstituted benzenesulfonamide bearing an unsubstituted amino group at the 4-position, used for the treatment of HIV infection. A second-generation HIV protease inhibitor, darunavir was designed to form robust interactions with the protease enzyme from many strains of HIV, including those from treatment-experienced patients with multiple resistance mutations to other protease inhibitors.		3.1610carbamate ester;
furofuran;
sulfonamide		antiviral drug;
HIV protease inhibitor
tacrolimus
Tacrolimus: A macrolide isolated from the culture broth of a strain of Streptomyces tsukubaensis that has strong immunosuppressive activity in vivo and prevents the activation of T-lymphocytes in response to antigenic or mitogenic stimulation in vitro.. tacrolimus (anhydrous) : A macrolide lactam containing a 23-membered lactone ring, originally isolated from the fermentation broth of a Japanese soil sample that contained the bacteria Streptomyces tsukubaensis.		1.9810macrolide lactambacterial metabolite;
immunosuppressive agent
amd 8664
[no description available]		3.1610
telaprevir
[no description available]		3.1610cyclopentapyrrole;
cyclopropanes;
oligopeptide;
pyrazines		antiviral drug;
hepatitis C protease inhibitor;
peptidomimetic
sirolimus
Sirolimus: A macrolide compound obtained from Streptomyces hygroscopicus that acts by selectively blocking the transcriptional activation of cytokines thereby inhibiting cytokine production. It is bioactive only when bound to IMMUNOPHILINS. Sirolimus is a potent immunosuppressant and possesses both antifungal and antineoplastic properties.. sirolimus : A macrolide lactam isolated from Streptomyces hygroscopicus consisting of a 29-membered ring containing 4 trans double bonds, three of which are conjugated. It is an antibiotic, immunosupressive and antineoplastic agent.		1.9810antibiotic antifungal drug;
cyclic acetal;
cyclic ketone;
ether;
macrolide lactam;
organic heterotricyclic compound;
secondary alcohol		antibacterial drug;
anticoronaviral agent;
antineoplastic agent;
bacterial metabolite;
geroprotector;
immunosuppressive agent;
mTOR inhibitor
biln 2061
BILN 2061: a macrocyclic NS3 protease inhibitor and antiviral agent; structure in first source		3.1610
n-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide
boceprevir : A synthetic tripeptide consisting of N-(tert-butylcarbamoyl)-3-methyl-L-valyl, a cyclopropyl-fused prolyl and 3-amino-4-cyclobutyl-2-oxobutanamide residues joined in sequence. Used for treatment of chronic hepatitis C virus genotype 1 infection.		3.1610tripeptide;
ureas		antiviral drug;
hepatitis C protease inhibitor;
peptidomimetic
danoprevir
[no description available]		3.1610
ulimorelin
ulimorelin: ghrelin agonist; an 18-membered macrocycle containing 3 amide bonds and a secondary amine as well as 4 stereogenic centers; belongs to macrocyclic peptidomimetics		3.1610oligopeptide
hirugen
hirugen: amino acid sequence given in first source		1.9910
simeprevir
[no description available]		3.1610azamacrocycle;
lactam
robotnikinin
robotnikinin: binds sonic hedgehog protein to block its signaling pathway; structure in first source		3.1610
hirudin
Hirudin: A 65-residue polypeptide from LEECHES.		1.9910
ConditionIndicatedRelationship StrengthStudiesTrials
Blood Clot
[description not available]		02.0110
Thrombosis
Formation and development of a thrombus or blood clot in the blood vessel.		02.0110
Asthma, Bronchial
[description not available]		02.0510
Asthma
A form of bronchial disorder with three distinct components: airway hyper-responsiveness (RESPIRATORY HYPERSENSITIVITY), airway INFLAMMATION, and intermittent AIRWAY OBSTRUCTION. It is characterized by spasmodic contraction of airway smooth muscle, WHEEZING, and dyspnea (DYSPNEA, PAROXYSMAL).		02.0510