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دانلود رایکان مقاله انگلیسی ISI با موضوع ساختار دارویی آلبومین سرم انسانی

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اساس ساختاری ویژگی دارویی آلبومین سرم انسانی

عنوان انگلیسی مقاله:

Structural Basis of the Drug-binding Specificity of Human Serum Albumin

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Structure determination and overview

HSA–drug and HSA-myristate–drug complexes were prepared either by co-crystallisation or crystal-soaking using relatively high (millimolar) drug concentrations, to help overcome the effect of the presence of w30% (v/v) polyethlyene glycol in the crystal and thereby ensure good occupancy (Materials and Methods; Supplementary Data). The structures of the drug complexes were solved by molecular replacement using previously determined structures of HSA16 or HSA-myristate4 as appropriate, since there were no gross conformational changes associated with drug binding. The shape of the difference electron density, coupled with consideration of the chemical nature of the binding environment, generally gave an unambiguous indication of the bound drug conformation (Figure 2). In a few cases, particularly complexes that were determined at lower resolutions (w3 A˚ ), refinement of alternative drug orientations was used to determine the most plausible conformation. Models for the various complexes were refined to resolutions of 2.25–3.20 A˚ and have Rfree values in the range 24.3–29.2% and good stereochemistry (Table 1).