title: Binding free energy calculations between bovine β-lactoglobulin and four fatty acids using the MMGBSA method.
abstract: The bovine dairy protein β-lactoglobulin (βlg) is a promiscuous protein that has the ability to bind several hydrophobic ligands. In this study, based on known experimental data, the dynamic interaction mechanism between bovine βlg and four fatty acids was investigated by a protocol combining molecular dynamics (MD) simulations and molecular mechanics generalized Born surface area (MMGBSA) binding free energy calculations. Energetic analyses revealed binding free energy trends that corroborated known experimental findings; larger ligand size corresponded to greater binding affinity. Finally, binding free energy decomposition provided detailed information about the key residues stabilizing the complex.
authors.affiliation: Laboratorio de Modelado Molecular y Bioinformática de la Escuela Superior de Medicina, Instituto Politécnico Nacional, México. Plan de San Luis Y Diaz Mirón S/N, Col. Casco de Santo Tomas, 11340 México, D. F., México.
authors.forename: Martiniano
authors.initials: M
authors.lastname: Bello
mesh_terms: D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D005227:Fatty Acids / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D013816:Thermodynamics
chemical_list: D005227:Fatty Acids; D007782:Lactoglobulins
keywords: capric acid; caprylic acid; free energy calculation; lactoglobulin; molecular dynamics; myristic acid; stearic acid