title: The neutral products formed during backbone fragmentations of protonated peptides in tandem mass spectrometry.
abstract: Collisionally activated dissociation (CAD) of the protonated polyalanines Ala-Ala,Ala-Ala-Ala, and Ala-Ala-Ala-Ala causes breakup of the peptide bonds leading to sequence-indicative fragment ions. The neutral molecules eliminated during these reactions are identified here using neutralization-reionization mass spectrometry (NRMS). N-terminal acylium ions (bn) arise after the C-terminus is lost as an intact amino acid or peptide; further loss of CO leads to immonium ions (an). Upon generation of C-terminal sequence ions (yn), a hydrogen atom attached to a nitrogen rearranges from the N-terminal to the C-terminal side yielding a protonated amino acid (y1) or peptide (y > or = 2) as the ionic fragment; the complementary neutral fragment is an aziridinone if the N-terminal amino acid is cleaved and a diketopiperazine if two N-terminal amino acid units are eliminated. Detection of neutral dissociation products can reveal valuable structure information, as demonstrated with the tetrapeptides Val-Gly-Ser-Glu and Val-Gly-Asp-Glu.
authors.affiliation: Department of Chemistry, University of Akron, Ohio 44325-3601.
authors.forename: M M
authors.initials: MM
authors.lastname: Cordero
authors.forename: J J
authors.initials: JJ
authors.lastname: Houser
authors.forename: C
authors.initials: C
authors.lastname: Wesdemiotis
mesh_terms: D000595:Amino Acid Sequence; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides; C019529:polyalanine