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• W2327195007 abstract "A new pseudopeptide epoxide inhibitor, designed for irreversible binding to HIV protease (HIV-PR), has been synthesized and characterized in solution and in the solid state. However, the crystal structure of the complex obtained by inhibitor-enzyme cocrystallization revealed that a minor isomer, with inverted configuration of the epoxide carbons, has been selected by HIV-PR during crystallization. The structural characterization of the well-ordered pseudopeptide, inserted in the catalytic channel with its epoxide group intact, provides deeper insights into inhibitor binding and HIV-PR stereoselectivity, which aids development of future epoxide-based HIV inhibitors." @default.
• W2327195007 created "2016-06-24" @default.
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• W2327195007 date "2014-07-17" @default.
• W2327195007 modified "2023-10-08" @default.
• W2327195007 title "Impact of Stereochemistry on Ligand Binding: X-ray Crystallographic Analysis of an Epoxide-Based HIV Protease Inhibitor" @default.
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• W2327195007 doi "https://doi.org/10.1021/ml500092e" @default.
• W2327195007 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4160752" @default.
• W2327195007 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25221650" @default.
• W2327195007 hasPublicationYear "2014" @default.
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