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• W2937135973 abstract "Glycosylation and phosphorylation are two important mechanisms in organism, both of which can finely regulate protein function respectively or simultaneously. Functional nanoprobes with various reversible interactions of aiming at glycan or phosphate group have been advanced dramatically, however, the comprehensive analysis towards them is largely restricted by the challenge to capture glycopeptides and phosphopeptides at the same time from complex samples due to the limitation of nanoprobe functionalization. Here, we fabricate a promising nanoprobe using the hydrophilic l-cysteine and titanium ions to enhance the phosphopeptides capture, meanwhile, realize the glycopeptides capture. We test the performance of the promising nanoprobe, showing that it is not only equipped with good unbiased ability in glycopeptides capture with high sensitivity and selectivity, but also highly effective for phosphopeptides capture. More importantly, the promising nanoprobe enables the simultaneous capture and analysis of glycosylated and phosphorylated peptides from mouse brain, as well as human eye lens of normal and cataract. The identification of glycosylated and phosphorylated sites within normal and cataract reflects their differential expression and offers an excellent insight to glycosylation/phosphorylation-related human eye diseases, indicating its great potential in glycoproteomics and phosphoproteomics researches." @default.
• W2937135973 created "2019-04-25" @default.
• W2937135973 creator A5042928549 @default.
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• W2937135973 date "2019-08-01" @default.
• W2937135973 modified "2023-10-16" @default.
• W2937135973 title "A promising nanoprobe based on hydrophilic interaction liquid chromatography and immobilized metal affinity chromatography for capture of glycopeptides and phosphopeptides" @default.
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• W2937135973 doi "https://doi.org/10.1016/j.aca.2019.04.010" @default.
• W2937135973 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31047140" @default.
• W2937135973 hasPublicationYear "2019" @default.
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