title: The parent anion of the RGD tripeptide: Photoelectron spectroscopy and quantum chemistry calculations.
abstract: The gas-phase conformation of the intact (parent) unprotected RGD(-) peptide anion has been investigated using a combination of anion photoelectron spectroscopy and quantum chemistry calculations of its low-energy stable structures. The experimentally observed RGD(-) species correspond to a conformation in which the guanidinium group is protonated, the C-terminus is neutral, the aspartic acid carboxyl is deprotonated, and the anion's excess electron orbital is localized on the protonated guanidinium. This structure is reminiscent of the RGD loop, which is the peptide motif recognized by trans-membrane integrins. The parent RGD(-) radical anion was generated using a unique infrared desorption-photoemission-helium jet ion source, whose ability to produce radical anions of peptides may also have analytical mass spectrometric implications.
authors.affiliation: Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: Xiang
authors.initials: X
authors.lastname: Li
authors.forename: Haopeng
authors.initials: H
authors.lastname: Wang
authors.forename: Kit H
authors.initials: KH
authors.lastname: Bowen
authors.forename: G
authors.initials: G
authors.lastname: Grégoire
authors.forename: F
authors.initials: F
authors.lastname: Lecomte
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Schermann
authors.forename: Charles
authors.initials: C
authors.lastname: Desfrançois
mesh_terms: D000838:Anions / Q000737:chemistry; D004583:Electrons; D005740:Gases / Q000737:chemistry; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D011789:Quantum Theory; D013057:Spectrum Analysis
chemical_list: D000838:Anions; D005740:Gases; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid