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Azadipeptide Nitriles: Highly Potent and Proteolytically Stable Inhibitors of Papain‐Like Cysteine Proteases
Author(s) -
Löser Reik,
Frizler Maxim,
Schilling Klaus,
Gütschow Michael
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200705858
Subject(s) - proteases , papain , cysteine , chemistry , cysteine protease , biochemistry , enzyme
Nitrogen instead of carbon : Azadipeptide nitriles resulting from CH/N exchange in the P 1 position (see picture) are hitherto unknown. To access these compounds by conversion of amino acid‐derived hydrazides with cyanogen bromide both nitrogen atoms of the hydrazide must be substituted. Despite a methylated P 2 ‐P 1 peptide bond, the azadipeptide nitriles show a strong inhibitory activity against cysteine proteases, and a high stability towards chymotryptic hydrolysis.