title: Specificity of ion-protein interactions: complementary and competitive effects of tetrapropylammonium, guanidinium, sulfate, and chloride ions.
abstract: The interactions of ions with a model peptide (a single melittin alpha-helix) in solutions of tetrapropylammonium sulfate or guanidinium chloride were examined by molecular dynamics simulations. The tetrapropylammonium cation shares the geometrical property of essentially flat faces with the previously examined guanidinium cation, and it was found that that this geometry leads to a strong preference for tetrapropylammonium to interact in a similar stacking-type fashion with flat nonpolar groups such as the indole side chain of tryptophan. In contrast to guanidinium, however, tetrapropylammonium does not exhibit strong ion pairing or clustering with sulfate counterions in the solution. Sulfate was found to interact almost exclusively and strongly with the cationic groups of the peptide, such that, already in a 0.1 m solution of tetrapropylammonium sulfate, the 6+ charge of the peptide is effectively locally neutralized. In combination with previous simulations, neutron scattering studies, and experiments on the conformational stability of model peptides, the present results suggest that the Hofmeister series can be explained in higher detail by splitting ions according to the effect they have on hydrogen bonding, salt bridges, and hydrophobic interactions in the protein and how these effects are altered by the counterion.
authors.affiliation: Department of Food Science, Cornell University, Ithaca, New York 14853, USA. pem27@cornell.edu
authors.forename: Philip E
authors.initials: PE
authors.lastname: Mason
authors.forename: Christopher E
authors.initials: CE
authors.lastname: Dempsey
authors.forename: Lubos
authors.initials: L
authors.lastname: Vrbka
authors.forename: Jan
authors.initials: J
authors.lastname: Heyda
authors.forename: John W
authors.initials: JW
authors.lastname: Brady
authors.forename: Pavel
authors.initials: P
authors.lastname: Jungwirth
mesh_terms: D000818:Animals; D001703:Biophysics / Q000379:methods; D002712:Chlorides / Q000737:chemistry*; D019295:Computational Biology / Q000379:methods; D003198:Computer Simulation; D019791:Guanidine / Q000737:chemistry*; D006860:Hydrogen Bonding; D007477:Ions; D008555:Melitten / Q000737:chemistry; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D000644:Quaternary Ammonium Compounds / Q000737:chemistry*; D012996:Solutions; D013431:Sulfates / Q000737:chemistry*
chemical_list: D002712:Chlorides; D007477:Ions; D010455:Peptides; D000644:Quaternary Ammonium Compounds; D012996:Solutions; D013431:Sulfates; C052377:tetrapropylammonium; D008555:Melitten; D019791:Guanidine