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On‐plate‐selective enrichment of glycopeptides using boronic acid‐modified gold nanoparticles for direct MALDI‐QIT‐TOF MS analysis
Author(s) -
Tang Jia,
Liu Yingchao,
Qi Dawei,
Yao Guoping,
Deng Chunhui,
Zhang Xiangmin
Publication year - 2009
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.200900033
Subject(s) - chromatography , boronic acid , glycopeptide , chemistry , detection limit , matrix assisted laser desorption/ionization , horseradish peroxidase , substrate (aquarium) , colloidal gold , matrix (chemical analysis) , nanoparticle , materials science , combinatorial chemistry , nanotechnology , adsorption , desorption , biochemistry , organic chemistry , oceanography , enzyme , geology , antibiotics
In this study, an on‐plate‐selective enrichment method is developed for fast and efficient glycopeptide investigation. Gold nanoparticles were first spotted and sintered on a stainless‐steel plate, then modified with 4‐mercaptophenylboronic acid to provide porous substrate with large specific surface and dual functions. These spots were used to selectively capture glycopeptides from peptide mixtures and the captured target peptides could be analyzed by MALDI‐MS simply by deposition of 2,5‐dihydroxybenzoic acid matrix. Horseradish peroxidase was employed as a standard glycoprotein to investigate the enrichment efficiency. In this way, the enrichment, washing and detection steps can all be fulfilled on a single MALDI target plate. The relatively small sample amount needed, low detection limit and rapid selective enrichment have made this on‐plate strategy promising for online enrichment of glycopeptides, which could be applied in high‐throughput proteome research.