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- W2066807686 abstract "Conformational analysis in solution of beta-secretase inhibitors 1 and 2 by NMR spectroscopy reveals that the hydroxyethylene isostere, an apparently flexible fragment widely used as a scissile bond replacement in aspartic protease inhibitors, exists in one predominant conformation in solution. This preferred conformation is similar to that adopted by the hydroxyethylene core of 1 in complex with beta-secretase and that adopted by hydroxyethylene cores of related compounds when bound to aspartic proteases, indicating that this structural unit is preorganized in solution." @default.
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- W2066807686 date "2005-11-02" @default.
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- W2066807686 title "Preorganization of the Hydroxyethylene Dipeptide Isostere: The Preferred Conformation in Solution Resembles the Conformation Bound to BACE" @default.
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- W2066807686 doi "https://doi.org/10.1021/jm050631+" @default.
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