title: Enantiospecific adsorption of amino acids on hydroxylated quartz (0001).
abstract: Density functional theory calculations have been used to study the adsorption of glycine, alanine, serine, and cysteine on the hydroxylated (0001) surface of alpha-quartz. We found negligible differences in adsorption energies for the most stable minima of enantiomers of alanine on this surface. There are, however, measurable energy differences between the two enantiomers of both serine and cysteine in their most stable states. The source of this enantiospecificity is mainly the difference in the strength of hydrogen bonds between the surface and the two enantiomers. Our results provide initial information on how amino acids can exhibit enantiospecific adsorption on hydroxylated quartz surfaces.
authors.affiliation: School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 311 Ferst Drive, Atlanta, Georgia 30332-0100, USA.
authors.forename: Jeong Woo
authors.initials: JW
authors.lastname: Han
authors.forename: David S
authors.initials: DS
authors.lastname: Sholl
mesh_terms: D000327:Adsorption; D000409:Alanine / Q000737:chemistry; D000596:Amino Acids / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D005998:Glycine / Q000737:chemistry; D006860:Hydrogen Bonding; D006900:Hydroxylation; D008958:Models, Molecular; D008968:Molecular Conformation; D011789:Quantum Theory; D011791:Quartz / Q000737:chemistry*; D012694:Serine / Q000737:chemistry; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D011791:Quartz; D012694:Serine; D003545:Cysteine; D000409:Alanine; D005998:Glycine