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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: A fast-field-cycling H-1-NMR relaxometric study
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Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: A fast-field-cycling H-1-NMR relaxometric study

机译：原型药物布洛芬和华法林对人血红素-白蛋白整体离液序列的影响：高速循环H-1-NMR弛豫研究

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摘要

Human serum albumin (HSA) is the most prominent protein in plasma, but it is also found in tissues and secretions throughout the body. The three-domain design of HSA provides a variety of binding sites for many ligands, including heme and drugs. HSA has been used as a model multidomain protein to investigate how interdomain interactions affect the global folding/unfolding process. Here, we report on the reversible chemical denaturation of heme-HSA involving three different conformational states (F, N, and B, occurring at pH 4.0, 7.0, and 9.0, respectively) and on the effect of prototypic drugs ibuprofen and warfarin on thermodynamics of the reversible unfolding process. Chaotropic unfolding of heme-HSA in the F, N, and B conformations is governed by different thermodynamic regimes, with the B form showing an entropic stabilization of the structure that compensates an enthalpic destabilization, and the F form easily unfolding under entropic control. Warfarin and ibuprofen binding stabilizes heme-HSA in both N and B states. (c) 2007 Elsevier B.V. All rights reserved.
机译：人血清白蛋白（HSA）是血浆中最突出的蛋白质，但也存在于人体的组织和分泌物中。 HSA的三结构域设计为许多配体（包括血红素和药物）提供了多种结合位点。 HSA已用作模型多域蛋白来研究域间相互作用如何影响全局折叠/展开过程。在这里，我们报道血红素-HSA的可逆化学变性涉及三种不同的构象状态（F，N和B，分别发生在pH 4.0、7.0和9.0），以及原型药物布洛芬和华法林对热力学的影响可逆的展开过程。 F，N和B构象中血红素-HSA的离液性展开受不同的热力学机制控制，其中B形式显示结构的熵稳定，补偿了焓的不稳定，F形式在熵控制下易于展开。华法林和布洛芬的结合可在N和B状态下稳定血红素-HSA。 （c）2007 Elsevier B.V.保留所有权利。

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