TY - JOUR
AU1 - CHEN, CHENG‐TAI
AU2 - CHEN, YU‐CHIE
AB -  Dear Sir, α‐Cyano‐4‐hydroxycinnamic acid (CHCA) is often selected as the matrix‐assisted laser desorption/ionization (MALDI) matrix for peptide analysis. However, CHCA is recognized as a hot matrix, 1–5 which is seldom used in the analysis of phosphopeptides. This is because extensive fragmentation from intact analytes is frequently observed in MALDI mass spectra when CHCA is used as the matrix. 6 , 7 However, fragmentation derived from phosphopeptides can provide data for confirmation of phosphorylation of unknown ions 7 , 8 after enrichment by the affinity probes. These results suggested an approach for confirmation of the presence of phosphorylated peptides simply by using CHCA as the MALDI matrix. 2,5‐dihydroxybenzoic acid (DHB) is the most common matrix for MALDI MS analysis of phosphopeptides. 9 , 10 The detection limit of phosphopeptides using 2,5‐DHB as the matrix is generally better than that of using CHCA. Unlike analytes homogeneously distributing among CHCA crystalline, inhomogeneous crystalline of 2,5‐DHB/analyte, i.e. ‘sweet spots’, is often observed during MALDI sample preparation. Although it is time‐consuming to search ‘sweet spots’ to obtain analyte signals, analytes are generally concentrated on specific spots, which, therefore, lower the detection limit of analytes when 2,5‐DHB is used as the MALDI matrix. Two 
TI - A two‐matrix system for MALDI MS analysis of serine phosphorylated peptides concentrated by Fe 3 O 4 /Al 2 O 3 magnetic nanoparticles
JF - Journal of Mass Spectrometry (Incorp Biological Mass Spectrometry)
DO - 10.1002/jms.1353
DA - 2008-04-01
UR - https://www.deepdyve.com/lp/wiley/a-two-matrix-system-for-maldi-ms-analysis-of-serine-phosphorylated-HDQB77aGpm
SP - 538
EP - 541
VL - 43
IS - 4
DP - DeepDyve
ER -