Highly specific phosphopeptide enrichment by titanium(IV) cross-linked chitosan composite

•High sensitive and selective phosphopeptides enrichment by titanium(IV) cross-linked chitosan composite (Ti-CTS).•Natural chitosan is applied for IMAC supporting material.•Phosphopeptides in standard proteins (casein variants) and two real samples (non-fat milk and serum) were well enriched by Ti-C...

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Published in:Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2016-01, Vol.1008, p.234-239
Main Authors: Wu, Ting, Shi, Jiani, Zhang, Chuanjing, Zhang, Lingfan, Du, Yiping
Format: Article
Language:English
Subjects:
Chitosan
Chitosan - chemistry
IMAC
MALDI TOF MS
Microscopy, Electron, Scanning
Phosphopeptide enrichment
Phosphopeptides - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Titanium - chemistry
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Summary:•High sensitive and selective phosphopeptides enrichment by titanium(IV) cross-linked chitosan composite (Ti-CTS).•Natural chitosan is applied for IMAC supporting material.•Phosphopeptides in standard proteins (casein variants) and two real samples (non-fat milk and serum) were well enriched by Ti-CTS. Natural chitosan was applied as supporting material for Ti(IV) based immobilized metal ion affinity chromatographic (IMAC) material (Ti-CTS). Compared with other polymer based IMAC, Ti-CTS can save the cockamamie synthesis procedures and be easy to obtain. The morphology, surface area, pore volume and elemental composition of Ti-CTS were revealed by scanning electron microscopy (SEM), Brunauer–Emmett–Teller (BET) method and X-ray photoelectron spectroscopy (XPS). Tryptic digest products from several standard proteins and two real samples (non-fat milk and serum) were enriched using Ti-CTS to demonstrate the efficiency of this method. The results showed that this composite enables high sensitive and selective phosphopeptide enrichment from casein variants, non-fat milk and human serum. Furthermore, multi-phosphorylated peptides with three serine phospholated sites (S*S*S*) demonstrated high affinity to Ti-CTS. Hence, this method had great potential for future studies of complex phosphoproteomes and especially multi-phosphorylated peptides.
ISSN:1570-0232
1873-376X
DOI:10.1016/j.jchromb.2015.11.051