title: Electron transfer dissociation reveals changes in the cleavage frequencies of backbone bonds distant to amide-to-ester substitutions in polypeptides.
abstract: Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Hansen
authors.forename: Hye R
authors.initials: HR
authors.lastname: Jung
authors.forename: Frank
authors.initials: F
authors.lastname: Kjeldsen
mesh_terms: D000577:Amides / Q000737:chemistry*; D000595:Amino Acid Sequence; D047630:Depsipeptides / Q000737:chemistry; D004583:Electrons; D006860:Hydrogen Bonding; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*
chemical_list: D000577:Amides; D047630:Depsipeptides; D007477:Ions; D010455:Peptides