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Cover Feature: Quantum Mechanics/Molecular Mechanics Studies of the Mechanism of Cysteine Proteases Inhibition by Dipeptidyl Nitroalkenes (Chem. Eur. J. 9/2020)
Author(s) -
Arafet Kemel,
González Florenci V.,
Moliner Vicent
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201905164
Subject(s) - proteases , cysteine , molecular mechanics , chemistry , nitroalkene , enzyme , mechanism (biology) , cysteine protease , biochemistry , stereochemistry , computational chemistry , molecular dynamics , physics , quantum mechanics , enantioselective synthesis , catalysis
A QM/MM computational study of the inhibition of three cysteine proteases suggests that the dipeptidyl nitroalkene Cbz‐Phe‐Ala‐CH=CH−NO 2 must be much more efficient in blocking the activity of the parasitic cysteine proteases than the human ones. Efforts focused on increasing the electrostatic interaction with the residues of the active site and the S2 pocket of these enzymes could be used as a guide to design new potent and selective inhibitors against parasitic cysteine proteases. More information can be found in the Full Paper by K. Arafet, F. V. González, and V. Moliner on page 2002.