title: Chirality-induced conformational preferences in peptide-metal ion binding revealed by IR spectroscopy.
abstract: Chirality reversal of a residue in a peptide can change its mode of binding to a metal ion, as shown here experimentally by gas-phase IR spectroscopy of peptide-metal ion complexes. The binding conformations of Li(+), Na(+), and H(+) with the LL and DL stereoisomers of PhePhe were compared through IR ion spectroscopy using the FELIX free-electron laser. For the DL isomer, both Li(+) and Na(+) exclusively coordinate to the amide O atom, the carboxyl O atom, and one of the aromatic rings (the OOR conformation), while for the LL isomer, a mixture of the OOR and NOR conformations was found. The stereochemically induced change in conformation is shown to reflect the strength of an NH···π interaction remote from the metal ion site. Protonated PhePhe shows no stereochemically induced variation in binding geometry.
authors.affiliation: Chemistry Department, Case Western Reserve University, Cleveland, Ohio 44106, United States. rcd@po.cwru.edu
authors.forename: Robert C
authors.initials: RC
authors.lastname: Dunbar
authors.forename: Jeffrey D
authors.initials: JD
authors.lastname: Steill
authors.forename: Jos
authors.initials: J
authors.lastname: Oomens
mesh_terms: D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008672:Metals, Alkali / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D013055:Spectrophotometry, Infrared; D013237:Stereoisomerism
chemical_list: D004151:Dipeptides; D008024:Ligands; D008672:Metals, Alkali; D011522:Protons; C026650:phenylalanylphenylalanine