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  • Title: Preorganization of the hydroxyethylene dipeptide isostere: the preferred conformation in solution resembles the conformation bound to BACE.
    Author: Vidal P, Timm D, Broughton H, Chen SH, Martín JA, Rivera-Sagredo A, McCarthy JR, Shapiro MJ, Espinosa JF.
    Journal: J Med Chem; 2005 Dec 01; 48(24):7623-7. PubMed ID: 16302802.
    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.
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