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

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Journal of the American Society for Mass Spectrometry

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.

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Authors and Affiliations

  1. Mass Spectrometry Laboratory, Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, 274-8510, Chiba, Japan

    Mitsuo Takayama

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  1. Mitsuo Takayama
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Correspondence to Mitsuo Takayama.

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Takayama, M. In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Am Soc Mass Spectrom 12, 420–427 (2001). https://doi.org/10.1016/S1044-0305(01)00218-5

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  • DOI: https://doi.org/10.1016/S1044-0305(01)00218-5

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