Page last updated: 2024-11-12

uamc00039

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

Description

UAMC00039: dipeptidyl peptidase II inhibitor; structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID11232124
CHEMBL ID98869
SCHEMBL ID6824340
MeSH IDM0500352

Synonyms (13)

Synonym
CHEMBL98869 ,
(s)-4-(4-chlorobenzylamino)-2-amino-1-(piperidin-1-yl)butan-1-one
2-(s)-amino-4-(4-chloro-benzylamino)-1-piperidin-1-yl-butan-1-one
bdbm50146972
n4-(4-chlorobenzyl)-2,4-diaminobutanoylpiperidine
uamc00039
(2s)-2-amino-4-[(4-chlorophenyl)methylamino]-1-piperidin-1-ylbutan-1-one
gtpl6538
SCHEMBL6824340
NCGC00379239-01
n-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(s)-butane-diamine
Q27089046
uamc-00039

Research Excerpts

Bioavailability

ExcerptReferenceRelevance
"The ATP-binding cassette transporter P-glycoprotein (P-gp) is known to limit both brain penetration and oral bioavailability of many chemotherapy drugs."( A High-Throughput Screen of a Library of Therapeutics Identifies Cytotoxic Substrates of P-glycoprotein.
Ambudkar, SV; Brimacombe, KR; Chen, L; Gottesman, MM; Guha, R; Hall, MD; Klumpp-Thomas, C; Lee, OW; Lee, TD; Lusvarghi, S; Robey, RW; Shen, M; Tebase, BG, 2019
)
0.51
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (7)

Potency Measurements

ProteinTaxonomyMeasurementAverage (µ)Min (ref.)Avg (ref.)Max (ref.)Bioassay(s)
cytochrome P450 2D6Homo sapiens (human)Potency10.68400.00108.379861.1304AID1645840
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Dipeptidyl peptidase 9Bos taurus (cattle)IC50 (µMol)76.60000.68000.68000.6800AID1501063
Dipeptidyl peptidase IVPorphyromonas gingivalisIC50 (µMol)100.00001.30001.30001.3000AID1501058
Dipeptidyl peptidase 4Homo sapiens (human)IC50 (µMol)171.20000.00010.444410.0000AID1501061; AID270814; AID343974; AID56227; AID611365
Dipeptidyl peptidase 4Homo sapiens (human)Ki0.00010.00000.34142.2000AID270814
Dipeptidyl peptidase 8Homo sapiens (human)IC50 (µMol)142.00000.00192.653210.0000AID1501062; AID270816; AID343972; AID611363
Dipeptidyl peptidase 9Homo sapiens (human)IC50 (µMol)77.60000.00011.420710.0000AID343973; AID611364
Dipeptidyl peptidase 2Homo sapiens (human)IC50 (µMol)0.00040.00020.93166.6000AID1501064; AID270815; AID343975; AID56221; AID611366
Dipeptidyl peptidase 2Homo sapiens (human)Ki0.00010.00010.09380.1250AID343975
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (25)

Processvia Protein(s)Taxonomy
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)
proteolysisDipeptidyl peptidase 8Homo sapiens (human)
apoptotic processDipeptidyl peptidase 8Homo sapiens (human)
immune responseDipeptidyl peptidase 8Homo sapiens (human)
negative regulation of programmed cell deathDipeptidyl peptidase 8Homo sapiens (human)
pyroptosisDipeptidyl peptidase 9Homo sapiens (human)
negative regulation of programmed cell deathDipeptidyl peptidase 9Homo sapiens (human)
proteolysisDipeptidyl peptidase 9Homo sapiens (human)
proteolysisDipeptidyl peptidase 2Homo sapiens (human)
lysosomal protein catabolic processDipeptidyl peptidase 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (12)

Processvia Protein(s)Taxonomy
serine-type peptidase activityDipeptidyl peptidase 9Bos taurus (cattle)
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 activityDipeptidyl peptidase 8Homo sapiens (human)
protein bindingDipeptidyl peptidase 8Homo sapiens (human)
serine-type peptidase activityDipeptidyl peptidase 8Homo sapiens (human)
dipeptidyl-peptidase activityDipeptidyl peptidase 8Homo sapiens (human)
aminopeptidase activityDipeptidyl peptidase 9Homo sapiens (human)
protein bindingDipeptidyl peptidase 9Homo sapiens (human)
serine-type peptidase activityDipeptidyl peptidase 9Homo sapiens (human)
dipeptidyl-peptidase activityDipeptidyl peptidase 9Homo sapiens (human)
identical protein bindingDipeptidyl peptidase 9Homo sapiens (human)
aminopeptidase activityDipeptidyl peptidase 2Homo sapiens (human)
serine-type peptidase activityDipeptidyl peptidase 2Homo sapiens (human)
serine-type exopeptidase activityDipeptidyl peptidase 2Homo sapiens (human)
dipeptidyl-peptidase activityDipeptidyl peptidase 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (22)

Processvia Protein(s)Taxonomy
plasma membraneDipeptidyl peptidase 9Bos taurus (cattle)
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)
cytoplasmDipeptidyl peptidase 8Homo sapiens (human)
cytoplasmDipeptidyl peptidase 8Homo sapiens (human)
cytosolDipeptidyl peptidase 8Homo sapiens (human)
cytosolDipeptidyl peptidase 9Homo sapiens (human)
nucleusDipeptidyl peptidase 9Homo sapiens (human)
cytosolDipeptidyl peptidase 9Homo sapiens (human)
microtubuleDipeptidyl peptidase 9Homo sapiens (human)
cell leading edgeDipeptidyl peptidase 9Homo sapiens (human)
extracellular regionDipeptidyl peptidase 2Homo sapiens (human)
Golgi apparatusDipeptidyl peptidase 2Homo sapiens (human)
azurophil granule lumenDipeptidyl peptidase 2Homo sapiens (human)
intracellular membrane-bounded organelleDipeptidyl peptidase 2Homo sapiens (human)
extracellular exosomeDipeptidyl peptidase 2Homo sapiens (human)
vesicleDipeptidyl peptidase 2Homo sapiens (human)
vesicleDipeptidyl peptidase 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (28)

Assay IDTitleYearJournalArticle
AID1501058Inhibition of Porphyromonas gingivalis N-terminal His-tagged DPP4 expressed in Escherichia coli using Gly-Pro-p-nitroanilide as substrate2017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID343975Inhibition of DPP22008Bioorganic & medicinal chemistry letters, Jul-15, Volume: 18, Issue:14
Inhibitors of dipeptidyl peptidase 8 and dipeptidyl peptidase 9. Part 1: identification of dipeptide derived leads.
AID270815Inhibition of DPP22006Bioorganic & medicinal chemistry letters, Sep-15, Volume: 16, Issue:18
Synthesis and dipeptidyl peptidase inhibition of N-(4-substituted-2,4-diaminobutanoyl)piperidines.
AID611366Inhibition of DPP22011Journal of medicinal chemistry, Aug-25, Volume: 54, Issue:16
Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
AID56227Inhibition of human Dipeptidylpeptidase IV (DPP IV)2004Journal of medicinal chemistry, May-20, Volume: 47, Issue:11
Gamma-amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl]piperidine as highly potent and selective dipeptidyl peptidase II inhibitors.
AID1501063Inhibition of bovine DPP92017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID343973Inhibition of DPP92008Bioorganic & medicinal chemistry letters, Jul-15, Volume: 18, Issue:14
Inhibitors of dipeptidyl peptidase 8 and dipeptidyl peptidase 9. Part 1: identification of dipeptide derived leads.
AID270817Selectivity for DPP2 over DPP42006Bioorganic & medicinal chemistry letters, Sep-15, Volume: 16, Issue:18
Synthesis and dipeptidyl peptidase inhibition of N-(4-substituted-2,4-diaminobutanoyl)piperidines.
AID611365Inhibition of DPP42011Journal of medicinal chemistry, Aug-25, Volume: 54, Issue:16
Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
AID611364Inhibition of DPP92011Journal of medicinal chemistry, Aug-25, Volume: 54, Issue:16
Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
AID235301Ratio of IC50 for DPP IV to that of IC50 for DPP II2004Journal of medicinal chemistry, May-20, Volume: 47, Issue:11
Gamma-amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl]piperidine as highly potent and selective dipeptidyl peptidase II inhibitors.
AID611363Inhibition of DPP82011Journal of medicinal chemistry, Aug-25, Volume: 54, Issue:16
Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
AID1501062Inhibition of DPP8 (unknown origin)2017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID1501061Inhibition of human DPP42017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID56221Inhibition of human Dipeptidylpeptidase II (DPP II)2004Journal of medicinal chemistry, May-20, Volume: 47, Issue:11
Gamma-amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl]piperidine as highly potent and selective dipeptidyl peptidase II inhibitors.
AID343972Inhibition of DPP82008Bioorganic & medicinal chemistry letters, Jul-15, Volume: 18, Issue:14
Inhibitors of dipeptidyl peptidase 8 and dipeptidyl peptidase 9. Part 1: identification of dipeptide derived leads.
AID343974Inhibition of DPP42008Bioorganic & medicinal chemistry letters, Jul-15, Volume: 18, Issue:14
Inhibitors of dipeptidyl peptidase 8 and dipeptidyl peptidase 9. Part 1: identification of dipeptide derived leads.
AID270818Selectivity for DPP2 over DPP82006Bioorganic & medicinal chemistry letters, Sep-15, Volume: 16, Issue:18
Synthesis and dipeptidyl peptidase inhibition of N-(4-substituted-2,4-diaminobutanoyl)piperidines.
AID270816Inhibition of DPP82006Bioorganic & medicinal chemistry letters, Sep-15, Volume: 16, Issue:18
Synthesis and dipeptidyl peptidase inhibition of N-(4-substituted-2,4-diaminobutanoyl)piperidines.
AID270814Inhibition of DPP42006Bioorganic & medicinal chemistry letters, Sep-15, Volume: 16, Issue:18
Synthesis and dipeptidyl peptidase inhibition of N-(4-substituted-2,4-diaminobutanoyl)piperidines.
AID1501064Inhibition of DPP2 (unknown origin)2017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID1501056Inhibition of Porphyromonas gingivalis N-terminal His-tagged DPP4 expressed in Escherichia coli at 10 uM using Gly-Pro-p-nitroanilide as substrate relative to control2017European journal of medicinal chemistry, Oct-20, Volume: 139Crystal structure of Porphyromonas gingivalis dipeptidyl peptidase 4 and structure-activity relationships based on inhibitor profiling.
AID1346986P-glycoprotein substrates identified in KB-3-1 adenocarcinoma cell line, qHTS therapeutic library screen2019Molecular pharmacology, 11, Volume: 96, Issue:5
A High-Throughput Screen of a Library of Therapeutics Identifies Cytotoxic Substrates of P-glycoprotein.
AID1347160Primary screen NINDS Rhodamine qHTS for Zika virus inhibitors2020Proceedings of the National Academy of Sciences of the United States of America, 12-08, Volume: 117, Issue:49
Therapeutic candidates for the Zika virus identified by a high-throughput screen for Zika protease inhibitors.
AID1296008Cytotoxic Profiling of Annotated Libraries Using Quantitative High-Throughput Screening2020SLAS discovery : advancing life sciences R & D, 01, Volume: 25, Issue:1
Cytotoxic Profiling of Annotated and Diverse Chemical Libraries Using Quantitative High-Throughput Screening.
AID1346987P-glycoprotein substrates identified in KB-8-5-11 adenocarcinoma cell line, qHTS therapeutic library screen2019Molecular pharmacology, 11, Volume: 96, Issue:5
A High-Throughput Screen of a Library of Therapeutics Identifies Cytotoxic Substrates of P-glycoprotein.
AID1347159Primary screen GU Rhodamine qHTS for Zika virus inhibitors: Unlinked NS2B-NS3 protease assay2020Proceedings of the National Academy of Sciences of the United States of America, 12-08, Volume: 117, Issue:49
Therapeutic candidates for the Zika virus identified by a high-throughput screen for Zika protease inhibitors.
AID1345410Human Dipeptidyl-peptidase 7 (S28: Lysosomal Pro-Xaa carboxypeptidase)2006Biochemical pharmacology, Jun-28, Volume: 72, Issue:1
Dipeptidyl peptidase II and leukocyte cell death.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (12)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's7 (58.33)29.6817
2010's3 (25.00)24.3611
2020's2 (16.67)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 (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other12 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]