Low-mass ions produced from peptides by high-energy collision-induced dissociation in tandem mass spectrometry

• Published in: Journal of the American Society for Mass Spectrometry Vol. 4; no. 11; pp. 882 - 893
• Main Authors: Falick, A.M., Hines, W.M., Medzihradszky, K.F., Baldwin, M.A., Gibson, B.W.
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 01.11.1993; Elsevier Science
• Subjects: Chemistry; Exact sciences and technology; Mass spectrometry; Organic chemistry; Reactivity and mechanisms; Collisional activation; Peptides; High energy; Aminoacid; Mass spectrometry MS/MS; Fragmentation pattern; Experimental study
• ISSN: 1044-0305; 1879-1123
• DOI: 10.1016/1044-0305(93)87006-X

High-energy collision-induced dissociation (CID) mass spectrometry provides a rapid and sensitive means for determining the primary sequence of peptides. The low-mass region (below mass 300) of a large number of tandem CID spectra of peptides has been analyzed. This mass region contains several types of informative fragment ions, including dipeptide ions, immonium ions, and other related ions. Useful low-mass ions are also present in negative-ion CID spectra. Immonium ions (general structure [H 2N=CH-R] +, where R is the amino acid side chain) and related ions characteristic of specific amino acid residues give information as to the presence or absence of these residues in the peptide being analyzed. Tables of observed immonium and related ions for the 20 standard amino acids and for a number of modified amino acids are presented. A database consisting of 228 high-energy CID spectra of peptides has been established, and the frequency of occurrence of various ions indicative of specific amino acid residues has been determined. Two model computer-aided schemes for analysis of the amino-acid content of unkown peptides have been developed and tested against the database.