Premium
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
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom