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In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Journal of the American Society for Mass Spectrometry (2001-04-27)
M Takayama
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 residues to ISD; however, the more sensitive residue(s) were not as clear. 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-bond 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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
ProteoMass ACTH Fragment 18-39 MALDI-MS Standard, vial of 10 nmol, monoisotopic mol wt 2,464.1989 Da
Sigma-Aldrich
Adrenocorticotropic Hormone Fragment 18-39 human, ≥97% (HPLC)

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