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Disappearance of interfering alkali‐metal adducted peaks from matrix‐assisted laser desorption/ionization mass spectra of peptides with serine addition to α ‐cyano‐4‐hydroxycinnamic acid matrix
Author(s) -
Nishikaze Takashi,
Takayama Mitsuo
Publication year - 2007
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.3219
Subject(s) - chemistry , matrix assisted laser desorption/ionization , mass spectrometry , desorption , mass spectrum , alkali metal , protonation , field desorption , analytical chemistry (journal) , ion , matrix (chemical analysis) , ionization , chromatography , organic chemistry , adsorption
It has been described that ion yield in both positive‐ and negative‐ion matrix‐assisted laser desorption/ionization mass spectrometry (MALDI MS) of peptides is often inhibited by trace amounts of alkali metals and that the MALDI mass spectra are contaminated by the interfering peaks originating from traces of alkali metals, even when sample preparation is carefully performed. Addition of serine to the commonly used MALDI matrix α ‐cyano‐4‐hydroxycinnamic acid (CHCA) significantly improved and enhanced the signals of both protonated and deprotonated peptides, [M+H] + and [M−H] − . The addition of serine to CHCA matrix eliminated the alkali‐metal ion adducts, [M+Na] + and [M+K] + , and the CHCA cluster ions from the mass spectra. Serine and serinephosphate as additives to CHCA enhanced and improved the formation of molecular‐related ions of phosphopeptides in negative‐ion MALDI mass spectra. Copyright © 2007 John Wiley & Sons, Ltd.