Targeted immobilization of titanium (IV) on magnetic mesoporous nanomaterials derived from metal-organic frameworks for
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ORIGINAL PAPER
Targeted immobilization of titanium (IV) on magnetic mesoporous nanomaterials derived from metal-organic frameworks for high-efficiency phosphopeptide enrichment in biological samples Chenlu Pu 1 & Hongli Zhao 1 & Qinying Gu 1 & Yu Zheng 1 & Minbo Lan 1,2 Received: 20 May 2020 / Accepted: 7 September 2020 # Springer-Verlag GmbH Austria, part of Springer Nature 2020
Abstract A selectively modified porous metal/carbon nanocomposite was fabricated to enhance the enrichment of low-abundance phosphopeptides from biological samples. The carbon matrix derived from the metal-organic framework provides a suitable pore size to allow the diffusion of peptides, while the deliberately modified metal nanoparticles within the pores enhance their interaction with the phosphopeptides. This nanocomposite shows extremely high enrichment selectivity for phosphopeptides in the MALDI-TOF MS detection, even when the molar ratio of α-casein digests versus bovine serum albumin digests was up to about 1:20,000. By combining such nanocomposite with nano-LC-MS/MS, 4556 unique phosphopeptides were identified with high selectivity (95.2%) from HeLa cell extracts. Furthermore, phosphopeptides from prostate tissue digests were also determined. A total of 277 and 1242 phosphopeptides were identified from normal and tumor tissues of a patient with prostate cancer, respectively. This indicates that phosphorylation and prostate cancer can be related to each other. Keywords Metal-organic frameworks . Mesoporous structure . Selective modification . Phosphopeptides enrichment . Mass spectrometry
Introduction Protein phosphorylation plays a central role in cellular regulation pathways, and divergences in phosphorylation in these regulatory pathways are related to the onset and progression of most cancer types. Characterizing phosphoproteins and identifying phosphorylation sites as comprehensively as possible
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00604-020-04556-5) contains supplementary material, which is available to authorized users. * Hongli Zhao [email protected] * Minbo Lan [email protected] 1
Shanghai Key Laboratory of Functional Materials Chemistry, School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, People’s Republic of China
2
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, People’s Republic of China
facilitate to understand diseased states and develop new drug targets [1]. Mass spectrometry (MS)-based peptide mapping is one of the basic tools for detecting phosphopeptides obtained from phosphoproteins, but phosphopeptides are difficult to detect in direct MS due to their low abundance and poor ionization performance compared with nonphosphopeptides [2]. Immobilized metal ion affinity chromatography (IMAC) is one of the most popular techniques for phosphopeptide enrichment [3]. Based on metal phosphonate chemistry, the capture of ph
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