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- W2042949672 abstract "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." @default.
- W2042949672 created "2016-06-24" @default.
- W2042949672 creator A5007314231 @default.
- W2042949672 creator A5049786321 @default.
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- W2042949672 date "2007-08-01" @default.
- W2042949672 modified "2023-10-16" @default.
- W2042949672 title "Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: A fast-field-cycling 1H-NMR relaxometric study" @default.
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- W2042949672 doi "https://doi.org/10.1016/j.bpc.2007.05.002" @default.
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