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Matrix‐free laser desorption/ionization of ions landed on plasma‐treated metal surfaces
Author(s) -
Volný Michael,
Sadílek Martin,
Jackson Karl E.,
Diener Matthew,
Elam W. Tim,
Tureček František
Publication year - 2008
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1402
Subject(s) - chemistry , gramicidin s , mass spectrometry , benzoic acid , desorption , ionization , analytical chemistry (journal) , pentapeptide repeat , ion , alkali metal , mass spectrum , metal , metal ions in aqueous solution , gramicidin , adsorption , chromatography , peptide , organic chemistry , biochemistry , membrane
We report new experiments in which laser desorption/ionization time‐of‐flight mass spectrometry (LDI‐TOF‐MS) was applied to detection and characterization of gramicidin S and IgG pentapeptide (DSDPR) that were reactively landed on plasma‐treated stainless steel surfaces. The distributions of [M + H] + , [M + Na] + and [M + K] + ion species in LDI‐TOF for gramicidin S and IgG pentapeptide (DSDPR) were found to be markedly different from those in conventional MALDI‐TOF spectra of the same samples. LDI‐TOF mass spectra showed a strong preference for [M + K] + adducts even in the presence of a large excess of sodium cations, or following surface treatment with trifluoroacetic acid. Alkali metal cations (K + and Cs + ) can be exchanged in reactively landed peptide samples to provide the corresponding cationized peptide ions by LDI. Multiple charged trypsin cations were reactively landed into a layer of 2‐(4‐hydroxyphenylazo)benzoic acid and ionized by LDI. The ionization mechanisms for LDI of surface‐deposited peptides are briefly discussed. Copyright © 2008 John Wiley & Sons, Ltd.