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On‐target and nanoparticle‐facilitated selective enrichment of peptides and proteins for analysis by MALDI ‐ MS
Author(s) -
Stolowitz Mark L.
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200252
Subject(s) - chemistry , mass spectrometry , matrix assisted laser desorption/ionization , chromatography , proteomics , nanoparticle , reagent , peptide , desorption , nanotechnology , combinatorial chemistry , materials science , adsorption , biochemistry , organic chemistry , gene
Over the course of the last decade, a number of investigators have come to appreciate that the surface of a MALDI target, after suitable modification, can be used for selective enrichment of peptides and proteins. More recently, surface‐modified nanoparticles ( NP s) that readily co‐crystallize in MALDI matrix, are not ionized by laser desorption/ionization, and do not interfere with MS have attracted interest as alternatives to surface‐modified targets for selective enrichment of peptides and proteins. Surface‐modified targets and NP s facilitate parallel processing of samples, and when used in conjunction with MALDI mass spectrometers with kHz lasers enable development of high‐throughput proteomics platforms. Targets and NP s for reversed phase and ion exchange retention, selective enrichment of glycopeptides, selective enrichment of phosphopeptides, and immunoaffinity MS are described in conjunction with details regarding their preparation and utility. Commercial availability of the reagents and substrates required to prepare surface‐modified targets and NP s is also discussed.