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Titanium (IV) ion-modified covalent organic frameworks for specific enrichment of phosphopeptides

Wang, Heping, Jiao, Fenglong, Gao, Fangyuan, Lv, Yayao, Wu, Qiong, Zhao, Yan, Shen, Yehua, Zhang, Yangjun, Qian, Xiaohong
Talanta 2017 v.166 pp. 133-140
Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, affinity chromatography, alpha-casein, beta-casein, detection limit, ligands, mass spectrometry, metal ions, proteomics, scanning electron microscopy, skim milk, titanium, transmission electron microscopy
To date, plenty of new alternative materials for phosphopeptides enrichment prior to mass spectrometry (MS) analysis appear, especially immobilized metal ion affinity chromatography (IMAC) materials. The variable combinations with different metal ions, chelating ligands and solid supports offer full of optionality for IMAC. However, further improvement was predicted by the tedious and complex synthetic process. In this work, a novel covalent organic framework (COF)-based IMAC material (denoted TpPa-2-Ti4+) was prepared simply by direct immobilizing Ti (IV) into TpPa-2 COFs without any extra chelating ligands. The structure and composition of as-prepared composites were confirmed by PXRD, FT-IR and XPS, and a new flower-shaped Ti4+-IMAC with regular micro-nano hierarchical structure was observed in the SEM and TEM images. The obtained titanium (IV) ion-modified covalent organic frameworks demonstrated low limit of detection (4 fmol) and largely-satisfactory selectivity (β-casein: BSA=1:100) for phosphopeptide capturing from β-casein. Similarly, 18 and 17 phosphopeptides could be easily detected in the tryptic digest of α-casein or the digest mixture of α-casein and BSA (1:50). They were also successfully applied for enrichment of phosphopeptides from non-fat milk and HeLa cells with high sensitivity and satisfactory selectivity. All above results showed that the new titanium (IV) ion-modified covalent organic framework is expected to be a potential IMAC for phosphopeptide enrichment in large-scale phosphoproteomics studies.