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Role of the Backbone Conformation at Position 7 in the Structure and Activity of Marinostatin, an Ester‐Linked Serine Protease Inhibitor
Author(s) -
Taichi Misako,
Yamazaki Toshimasa,
Nishiuchi Yuji
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200315
Subject(s) - proteases , serine protease , stereochemistry , serine , amide , chemistry , protease , position (finance) , olefin fiber , biochemistry , enzyme , finance , economics , catalysis
Rational design of inhibitors: The cis ‐amide backbone at position 7 in the serine protease inhibitor marinostatin was replaced with an E or Z olefin. The E olefin analogue was not active, but the Z analogue was. The cis conformation might play a critical role in organizing a canonical structure for binding to proteases.