SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach.
We report on the solvation properties and intermolecular interactions of a model protein (bovine serum albumine, BSA) in urea aqueous solutions, as obtained by combining small-angle neutron and X-ray scattering experiments. According to a global fit strategy, all the whole set of scattering curves are analysed by considering a unique model which includes the BSA structure, the protein-protein interactions and the thermodynamic exchange process of water/urea molecules at the protein solvent interface. As a main result, the equilibrium constant that accounts for the difference in composition between the bulk solvent and the protein solvation layer is derived. Results confirm that urea preferentially sticks to the protein surface, inducing a noticeable change in both the repulsive and the attractive interaction potentials.
Sinibaldi
Raffaele
R
Dipartimento di Scienze applicate ai Sistemi Complessi, Università Politecnica delle Marche, Via Brecce Bianche, 60019 Ancona, Italy. r.sinibaldi@alisf1.univpm.it
Ortore
Maria Grazia
MG
Spinozzi
Francesco
F
de Souza Funari
Sérgio
S
Teixeira
José
J
Mariani
Paolo
P
D000818:Animals; D002417:Cattle; D008958:Models, Molecular; D033363:Neutron Diffraction; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D053838:Scattering, Small Angle; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions; D012997:Solvents / Q000737:chemistry*; D013816:Thermodynamics; D014508:Urea / Q000737:chemistry* / Q000494:pharmacology; D014867:Water / Q000737:chemistry*; D014961:X-Ray Diffraction
D012996:Solutions; D012997:Solvents; D014867:Water; D012710:Serum Albumin, Bovine; D014508:Urea