title: Fatty acid binding to serum albumin: molecular simulation approaches.
abstract: BACKGROUND
  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.
  
  
  METHODS
  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.
  
  
  CONCLUSIONS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Biological Regulation, Faculty of Medicine, Tottori University, 86 Nishi-cho, Yonago 683-8503, Japan. Electronic address: fujiwara@med.tottori-u.ac.jp.
authors.forename: Shin-ichi
authors.initials: S
authors.lastname: Fujiwara
authors.forename: Takashi
authors.initials: T
authors.lastname: Amisaki
mesh_terms: D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D005227:Fatty Acids; D012709:Serum Albumin
keywords: Docking; Fatty acid; Free energy; Human serum albumin; Molecular dynamics; Simulation