Journal
JOURNAL OF PROTEOME RESEARCH
Volume 6, Issue 12, Pages 4763-4769Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr0705284
Keywords
phosphorylated peptides; enrichment; TiO2; nanoparticles; MALDI-TOF MS
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An on-plate specific enrichment method is presented for the direct analysis of pepticles phosphorylation. An array of sintered TiO2 nanoparticle spots was prepared on a stainless steel plate to provide porous substrate with a very large specific surface and durable functions. These spots were used to selectively capture phosphorylated pepticles from peptide mixtures, and the immobilized phosphopeptides could then be analyzed directly by MALDI MS after washing away the nonphosphorylated pepticles. beta-Casein and protein mixtures were employed as model samples to investigate the selection efficiency. In this strategy, the steps of phosphopeptide capture, purification, and subsequent mass spectrometry analysis are all successfully accomplished on a single target plate, which greatly reduces sample loss and simplifies analytical procedures. The low detection limit, small sample size, and rapid selective entrapment show that this on-plate strategy is promising for online enrichment of phosphopeptides, which is essential for the analysis of minute amount of samples in high-throughput proteome research.
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