Synthesis and Structure–activity Relationship of N-alkyl Gly-boro-Pro Inhibitors of DPP4, FAP, and DPP7
Y Hu, L Ma, M Wu, MS Wong, B Li, S Corral… - Bioorganic & Medicinal …, 2005 - Elsevier
Y Hu, L Ma, M Wu, MS Wong, B Li, S Corral, Z Yu, T Nomanbhoy, S Alemayehu, SR Fuller…
Bioorganic & Medicinal Chemistry Letters, 2005•ElsevierThe 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-α (FAP) optimally preferred N-cycloheptyl whereas DPP7
tolerated even larger cycloalkyl rings. Gly α-carbon derivatization of N-cyclohexyl or N-(2-
adamantyl) Gly-boro-Pro resulted in a significant decrease in potency against all the three
DPPs.
dipeptidyl peptidases (DPPs) was studied. In a series of N-cycloalkyl analogs, DPP4 and
fibroblast activation protein-α (FAP) optimally preferred N-cycloheptyl whereas DPP7
tolerated even larger cycloalkyl rings. Gly α-carbon derivatization of N-cyclohexyl or N-(2-
adamantyl) Gly-boro-Pro resulted in a significant decrease in potency against all the three
DPPs.
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-α (FAP) optimally preferred N-cycloheptyl whereas DPP7 tolerated even larger cycloalkyl rings. Gly α-carbon derivatization of N-cyclohexyl or N-(2-adamantyl) Gly-boro-Pro resulted in a significant decrease in potency against all the three DPPs.
Elsevier
