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Titolo:
In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Autore:
Takayama, M;
Indirizzi:
Toho Univ, Mass Spectrometry Lab, Funabashi, Chiba 2748510, Japan Toho Univ Funabashi Chiba Japan 2748510 , Funabashi, Chiba 2748510, Japan
Titolo Testata:
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
fascicolo: 4, volume: 12, anno: 2001,
pagine: 420 - 427
SICI:
1044-0305(200104)12:4<420:IDCOPI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLISION-INDUCED DISSOCIATION; ELECTRON-CAPTURE DISSOCIATION; DIRECT-SEQUENCE ANALYSIS; SOURCE FRAGMENTATION; DESORPTION-IONIZATION; POSTSOURCE DECAY; PROTEINS; MALDI; IONS; EXTRACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Takayama, M Toho Univ, Mass Spectrometry Lab, 2-2-1 Miyama, Funabashi, Chiba 2748510, Japan Toho Univ 2-2-1 Miyama Funabashi Chiba Japan 2748510 10, Japan
Citazione:
M. Takayama, "In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry", J AM SOC M, 12(4), 2001, pp. 420-427

Abstract

In-source decay (ISD) of peptides, coupled with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, has been examined to determine the influence of the matrix, the susceptibility of amino-acid residues to ISD, and the effect of extraction delay times. Out of nine di- and tri-hydroxybenzoic acids and three cinnamic derivatives tested, the most suitable matrix for ISD was 2,5-dihydroxybenzoic acid. The amine bond at Xxx-Gly and Xxx-Val residues was less susceptible than other amino-acid residuesto ISD; however, the more sensitive residue(s) were not as dear. Using a peptide that gave the y(n)- and (z(n) + 2)-series product ions, it was confirmed that amide-bond cleavage (formation of the y(n)-series ions) accompanied metastable peaks, whereas metastable peaks were never observed with amine-bond cleavage [formation of the (z(n) + 2)-series ions]. Furthermore, abundant c(n)-series ions, which originate from amine-hond cleavage on the peptide backbone, were observed whenever a minimum delay time of 38 ns or continuous extraction was used to obtain spectra. These data indicate that amine-bond cleavage in ISD takes place on the ionization time scale before the energy randomization is completed. (C) 2001 American Society for Mass Spectrometry.

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Documento generato il 04/07/20 alle ore 21:24:58