| Literature DB >> 18598016 |
Milan Kozísek1, Petr Cígler, Martin Lepsík, Jindrich Fanfrlík, Pavlína Rezácová, Jirí Brynda, Jana Pokorná, Jaromír Plesek, Bohumír Grüner, Klára Grantz Sasková, Jana Václavíková, Vladimír Král, Jan Konvalinka.
Abstract
HIV protease (PR) is a prime target for rational anti-HIV drug design. We have previously identified icosahedral metallacarboranes as a novel class of nonpeptidic protease inhibitors. Now we show that substituted metallacarboranes are potent and specific competitive inhibitors of drug-resistant HIV PRs prepared either by site-directed mutagenesis or cloned from HIV-positive patients. Molecular modeling explains the inhibition profile of metallacarboranes by their unconventional binding mode.Entities:
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Year: 2008 PMID： 18598016 DOI： 10.1021/jm8002334
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446