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Peptide‐Biphenyl Hybrids as Calpain Inhibitors
Author(s) -
Montero Ana,
Mann Enrique,
Chana Antonio,
Herradón Bernardo
Publication year - 2004
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200490037
Subject(s) - calpain , chemistry , peptide , biphenyl , cysteine protease , biochemistry , hybrid , cysteine , ic50 , protease , stereochemistry , in vitro , enzyme , biology , organic chemistry , botany
Calpain is a cysteine protease that is activated by Ca 2+ . The over‐activation of calpain, which occurs on increasing Ca 2+ concentration, causes a variety of diseases. This paper reports experimental results on the inhibition of calpain I ( μ‐ calpain) by peptidebiphenyl hybrids. We have found that some peptidebiphenyl hybrids, with aromatic amino acids in the peptide chains, inhibit calpain with IC 50 values in the nanomolar range. Since the peptidebiphenyl hybrids reported in the present paper do not posses a reactive electrophilic functionality, we hypothesize that they interfere with the activation of calpain by Ca 2+ , and present experimental and computational results on the binding of peptidebiphenyl hybrids to Ca 2+ .