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Design, Synthesis, and Preliminary Activity Evaluation of Novel Peptidomimetics as Aminopeptidase N/CD13 Inhibitors
Author(s) -
Li Xun,
Wang Junli,
Zhang Lei,
Xu Wenfang
Publication year - 2011
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.201100109
Subject(s) - peptidomimetic , chemistry , enzyme , amide , matrix metalloproteinase , matrix metalloproteinase inhibitor , stereochemistry , aminopeptidase , structure–activity relationship , enzyme inhibitor , biochemistry , combinatorial chemistry , in vitro , pharmacology , amino acid , peptide , biology , leucine
Abstract The synthesis of a series of novel N ‐α‐galloylated isoglutamic acid γ‐amide peptidomimetics is described. Their enzymatic inhibition against aminopeptidase N (APN/CD13) and matrix metalloproteinase‐2 (MMP‐2) was tested. The preliminary activity assay revealed that most of the compounds displayed selective inhibition against APN as compared with MMP‐2, with IC 50 values in a micromolar range. Within this series, compound 4 (IC 50 = 10.2 ± 0.9 µM) demonstrated comparable APN inhibition as compared with the positive control bestatin (IC 50 = 13.1 ± 0.7 µM), which might be a promising lead for further molecular optimizations.