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J Med Chem. 2014 Dec 11;57(23):10198-204. doi: 10.1021/jm5015633. Epub 2014 Nov 21.

Analysis of subpocket selectivity and identification of potent selective inhibitors for matriptase and matriptase-2.

Author information

1
Departments of Biochemistry and ‡Pharmacology, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001 12e Avenue Nord, Sherbrooke, Quebec J1H 5N4, Canada.

Abstract

We studied the factors affecting the selectivity of peptidomimetic inhibitors of the highly homologous proteases matriptase and matriptase-2 across subpockets using docking simulations. We observed that the farther away a subpocket is located from the catalytic site, the more pronounced its role in selectivity. As a result of our exhaustive virtual screening, we biochemically validated novel potent and selective inhibitors of both enzymes.

PMID:
25387268
DOI:
10.1021/jm5015633
[Indexed for MEDLINE]

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