Comparison between the matrices alpha-cyano-4-hydroxycinnamic acid and 4-chloro-alpha-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry.

作者: Thorsten W. Jaskolla , Dimitrios G. Papasotiriou , Michael Karas

DOI: 10.1021/PR900274S

关键词: PepsinChymotrypsinalpha-Cyano-4-hydroxycinnamic acidPeptideChromatographyChemistryProtein mass spectrometryProteaseIsoelectric pointTrypsin

摘要: The performance of the recently developed 4-chloro-α-cyanocinnamic acid (Cl-CCA) matrix-assisted laser desorption ionization mass spectrometry (MALDI MS) matrix was investigated in comparison to most widely used α-cyano-4-hydroxycinnamic (CHCA). For this purpose, in-solution digestions standard proteins low femtomole range with proteases trypsin, chymotrypsin, and pepsin were as analytes. all protein−protease combinations, Cl-CCA revealed be highly superior terms number identified peptides, obtained sequence coverages peptide detection reproducibility. A deeper inspection detected signals regard both physicochemical properties (their isoelectric point) spectrometric (signal-to-noise ratios accuracies) showed that progress achieved is due numerous acidic neutral peptides. Moreover, higher sensitivity allowed for addit...

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