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Updated: Jun 8, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Surface-modified TiO(2) nanoparticles as affinity probes and as matrices for the rapid analysis of phosphopeptides
Yaotang Ke1, Suresh Kumar Kailasa, Hui-Fen Wu
1Department of Chemistry, National Sun Yat-Sen University, Kaohsiung, Taiwan.
Abstract:
We utilized three different types of TiO(2) nanoparticles (NPs) namely TiO(2)-dopamine, TiO(2)-CdS and bare TiO(2) NPs as multifunctional nanoprobes for the rapid enrichment of phosphopeptides from tryptic digests of α- and β-casein, milk and egg white using a simplified procedure in MALDI-TOF-MS. Surface-modified TiO(2) NPs serve as effective matrices for the analysis of peptides (gramicidin D, HW6, leucine-enkephalin and methionine-enkephalin) and proteins (cytochrome c and myoglobin) in MALDI-TOF-MS. In the surface-modified TiO(2) NPs-based MALDI mass spectra of these analytes (phosphopetides, peptides and proteins), we found that TiO(2)-dopamine and bare TiO(2) NPs provided an efficient platform for the selective and rapid enrichment of phosphopeptides and TiO(2)-CdS NPs efficiently acted as the matrix for background-free detection of peptides and proteins with improved resolution in MALDI-MS. We found that the upper detectable mass range is 17 000 Da using TiO(2)-CdS NPs as the matrix. The approach is simple and straightforward for the rapid analysis of phosphopeptides, peptides and proteins by MALDI-MS in proteome research.
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