| Literature DB >> 16085416 |
Yi Hu1, 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.
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.Entities:
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Year: 2005 PMID： 16085416 DOI： 10.1016/j.bmcl.2005.06.075
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823