Authors
Yi Hu, Lifu Ma, Min Wu, Melissa S Wong, Bei Li, Sergio Corral, Zhizhou Yu, Tyzoon Nomanbhoy, Senaiet Alemayehu, Stacy R Fuller, Jonathan S Rosenblum, Natasha Rozenkrants, Lauro C Minimo, William C Ripka, Anna K Szardenings, John W Kozarich, Kevin R Shreder
Publication date
2005/10/1
Journal
Bioorganic & Medicinal Chemistry Letters
Volume
15
Issue
19
Pages
4239-4242
Publisher
Pergamon
Description
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.
Total citations
Scholar articles
Y Hu, L Ma, M Wu, MS Wong, B Li, S Corral, Z Yu… - Bioorganic & Medicinal Chemistry Letters, 2005