Abstract
The structure-activity relationship of various N-alkyl Gly-boro-Pro derivatives against three dipeptidyl peptidases (DPPs) was studied. In a series of N-cycloalkyl analogs, DPP4 and fibroblast activation protein-alpha (FAP) optimally preferred N-cycloheptyl whereas DPP7 tolerated even larger cycloalkyl rings. Gly alpha-carbon derivatization of N-cyclohexyl or N-(2-adamantyl) Gly-boro-Pro resulted in a significant decrease in potency against all the three DPPs.
MeSH terms
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Adenosine Deaminase Inhibitors
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Antigens, Neoplasm
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Biomarkers, Tumor / antagonists & inhibitors
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Boronic Acids
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Dipeptides / chemical synthesis*
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Dipeptides / pharmacology
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Dipeptidyl Peptidase 4
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / antagonists & inhibitors*
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Endopeptidases
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Gelatinases
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Glycoproteins / antagonists & inhibitors
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Humans
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Immunologic Factors / chemical synthesis
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Immunologic Factors / pharmacology
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Inhibitory Concentration 50
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Membrane Proteins
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Serine Endopeptidases
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Structure-Activity Relationship
Substances
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Adenosine Deaminase Inhibitors
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Antigens, Neoplasm
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Biomarkers, Tumor
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Boronic Acids
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Dipeptides
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Glycoproteins
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Immunologic Factors
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Membrane Proteins
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Endopeptidases
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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dipeptidyl peptidase II
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DPP4 protein, human
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Dipeptidyl Peptidase 4
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Serine Endopeptidases
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fibroblast activation protein alpha
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Gelatinases