bba1830(12)_5427.pdf 933 KB
Fujiwara, Shin-ichi Department of Biological Regulation, Faculty of Medicine, Tottori University Researchers DB KAKEN
Human serum albumin
Binding affinity for human serum albumin (HSA) is one of the most important factors affecting the distribution and free blood concentration of many ligands. The effect of fatty acids (FAs) on HSA-ligand binding has long been studied. Since the elucidation of the 3-dimensional structure of HSA, molecular simulation approaches have been applied to studies of the structure-function relationship of HSA-FA binding.
Scope of review
We review current insights into the effects of FA binding on HSA, focusing on the biophysical insights obtained using molecular simulation approaches such as docking, molecular dynamics (MD), and binding free energy calculations.
Possible conformational changes on binding of FA molecules to HSA have been observed through MD simulations. High- and low-affinity FA-binding sites on HSA have been identified based on binding free energy calculations. The relationship between the warfarin binding affinity of HSA and FA molecules has been clarified based on the results of simulations of multi-site FA binding that cannot be experimentally observed.
Molecular simulation approaches have great potentials to provide detailed biophysical insights into HSA as well as the effects of the binding of FAs or other ligands to HSA. This article is part of a Special Issue entitled Serum Albumin.
Biochimica et biophysica acta. General subjects : BBA
Copyright © 2013 Elsevier B.V. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/
Shin-ichi Fujiwara, Takashi Amisaki.. Fatty acid binding to serum albumin: Molecular simulation approaches. Biochimica et biophysica acta. General subjects : BBA. 2013, 1830(12), 5427-5434
Faculty of Medicine/Graduate School of Medical Sciences/University Hospital