Structural basis of the drug-binding specificity of human serum albumin.
@article{Ghuman2005StructuralBO, title={Structural basis of the drug-binding specificity of human serum albumin.}, author={Jamie Ghuman and Patricia A. Zunszain and Isabelle Petitpas and Ananyo A. Bhattacharya and Masaki Otagiri and Stephen Curry}, journal={Journal of molecular biology}, year={2005}, volume={353 1}, pages={ 38-52 } }
1,399 Citations
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The modulation of ligand binding to HSA is relevant not only under physiological conditions, but also in the pharmacological therapy management as several factors can modulate drug binding.
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This review deals with one of the protein's major binding sites "Sudlow I" which includes a binding pocket for the drug warfarin (WAR), and highlights the nature of Sudlow I as a flexible binding site, capable of binding a variety of ligands by adapting its binding pockets.
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A topology analysis of drug binding sites on HSA and AGP was determined using various methods, including spectroscopy, QSAR, photoaffinity labeling and site directed mutagenesis, and Recombinant albumin was found to be useful for rapidly identifying drugbinding sites.
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The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins.
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- Biology, ChemistryInternational journal of molecular sciences
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This review will succinctly outline the properties of binding site of drugs in IIA subdomain within the structure of HSA to give an overview on the binding characterization of interactive association of drugs to human serum albumin that may potentially lead to significant clinical applications.
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A computational-based molecular docking approach incorporating AutoDock Vina may prove useful to the prediction of the binding affinities of drugs towards human serum albumin, and thus, could help alleviate a major bottleneck of the drug discovery process.
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It is suggested that albumin binding should be taken into careful consideration in antimicrobial peptide studies, as the systemic distribution can be significantly affected by HSA interactions.
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This review focuses on the combination of biochromatography and circular dichroism as an effective approach for the characterization of albumin binding sites and their enantioselectivity.
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The previously determined crystal structure of the bacterial albumin-binding GA module in complex with human serum albumin (HSA) suggested the possibility of utilizing the complex in the study of ligand binding to HSA, and structure comparisons with solved structures of HSA and of the HSA-GA complex show that the GA module is capable of binding to different conformations of H SA.
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