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A fast, reproducible and low‐cost method for sequence deconvolution of ‘on‐bead’ peptides via ‘on‐target’ maldi‐TOF/TOF mass spectrometry
Author(s) -
Amadei Giulio A.,
Cho ChoiFong,
Lewis John D.,
Luyt Leonard G.
Publication year - 2010
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.1708
Subject(s) - chemistry , mass spectrometry , peptide , linker , chromatography , matrix assisted laser desorption/ionization , pentamer , polystyrene , maldi imaging , deconvolution , combinatorial chemistry , desorption , polymer , adsorption , algorithm , biochemistry , organic chemistry , computer science , operating system
A novel approach to high‐throughput sequence deconvolution of on‐bead small peptides (MW < 2000 Da) using on‐target MALDI‐TOF/TOF instrumentation is presented. Short peptides of pentamer and octamer length, covalently attached to TentaGel polystyrene beads through a photolabile linker, were placed onto the MALDI target, apportioned with suitable matrix (2,5‐dihydroxybenzoic acid) and then hit with the instrument laser (Nd : YAG, 355 nm). This induced easy and highly reproducible photochemical cleavage, desorption (MS mode) and fragmentation (MS/MS mode). Peptide fragments were identified with a mass accuracy of 0.1 Da of the expected values. This technique significantly accelerates the sequence determination of positive peptide hits obtained from random combinatorial libraries when screening against biological targets, paving the way for a rapid and efficient method to identify molecular imaging ligands specific to pathological targets in cancer and other diseases. Copyright © 2009 John Wiley & Sons, Ltd.