Linked Life Data

8825619

Source:http://linkedlifedata.com/resource/pubmed/id/8825619

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pubmed-article:8825619pubmed:abstractTextInhibitors of HIV-1 protease represent a new class of antiretroviral compounds. Here, we report the design and synthesis of two novel C2 symmetry-based inhibitors, MP-134 and MP-167, specifically targeted against HIV-1 variants with reduced sensitivity to another related protease inhibitor, A-77003. In addition, we describe the in vitro selection of viral variants with reduced sensitivity of these two protease inhibitors. An isoleucine-to-valine substitution at residue 84 (I84V) of the HIV-1 protease confers resistance to MP-134, whereas a glycine-to-valine substitution at residue 48 (G48V) confers resistance to MP-167. Testing other protease inhibitors against these variants has revealed specific overlapping patterns of resistance among these agents. These findings have important implications in the design of combination regimens using multiple protease inhibitors and underscore the need to develop non-cross-resistant compounds to be used toward this goal.lld:pubmed
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pubmed-article:8825619pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:8825619pubmed:year1996lld:pubmed
pubmed-article:8825619pubmed:articleTitleDesign, synthesis, and resistance patterns of MP-134 and MP-167, two novel inhibitors of HIV type 1 protease.lld:pubmed
pubmed-article:8825619pubmed:affiliationAaron Diamond AIDS Research Center, New York University School of Medicine, New York 10016, USA.lld:pubmed
pubmed-article:8825619pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8825619pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:8825619pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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