Synthesis of Al3+-doping-TiO2 monodisperse microspheres and their application for phosphopeptides and glycopeptides enrichment

Synthesis of Al3+-doping-TiO2 monodisperse microspheres and their application for phosphopeptides and glycopeptides enrichment
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Al3掺杂TiO2单分散微球的合成及其在磷酸肽和糖肽富集中的应用

DOI:
10.1016/j.talanta.2020.121715
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发表时间:
2020
期刊:
影响因子:
6.1
通讯作者:
Minbo Lan
Minbo Lan
中科院分区:
化学1区
文献类型:
--
作者:
Qianying Sheng;Chenli Xue;Yang Zhou;Junyan Li;Huihui Yuan;Yanxiong Ke;Minbo Lan

文献摘要

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糖基化和磷酸化是蛋白质翻译后修饰中最常见和最重要的两种,在调节多种复杂的生物学过程和参与多种疾病中起着重要作用。由于磷酸肽和糖肽的丰度低,高选择性富集方法对于通过质谱(MS)鉴定蛋白质磷酸化和糖基化至关重要。在此条件下,可以制备出单分散均匀的Al 3+掺杂-TiO 2复合氧化物微球。在水热处理过程中,通过溶胶-凝胶法控制形貌。采用SEM、TEM、XRD和N2吸附-脱附等温线对所得微球进行了表征。采用不同的富集条件,将Al 3+掺杂TiO 2分别或同时用于糖肽和磷酸肽的富集,实现了对糖肽和磷酸肽的选择性富集。从人血清IgG和α-酪蛋白(摩尔比为1:1)的胰蛋白酶消化混合物中富集的20个糖肽和25个磷酸肽明显可见,信噪比(S/N)大大提高。同时,脱脂牛奶和人血清的富集结果也显示了对复杂生物样品的富集选择性。本研究为翻译后修饰蛋白质组学研究中糖肽和磷酸肽的选择性富集提供了新的思路。
Glycosylation and phosphorylation are two of the most common and important post-translational modifications (PTMs) of proteins, which play critical roles in regulating a variety of complex biological processes and involvement in many diseases. Due to the low abundance of phosphopeptides and glycopeptides, highly selective enrichment methods are crucial to the identification of protein phosphorylation and glycosylation by mass spectrometry (MS). Here, monodisperse uniform Al3+-doping-TiO2mixed oxide microspheres were easily synthesized. The morphology was controlled by a sol-gel method, during the hydrothermal treatment. The obtained microspheres with uniform particle size distribution (about 1–2 μm),high surface area and improved pore structures, were characterized by SEM, TEM, XRD and N2adsorption-desorption isotherms. Al3+-doping-TiO2was applied in enriching glycopeptides and phosphopeptides respectively or simultaneously by using different enrichment conditions, achieving selective enrichment of glycopeptides and phosphopeptides. 20 glycopeptides and 25 phosphopeptides enriched from the tryptic digest mixtures of human serum immunoglobulin G (IgG) and α-casein (molar ratio of 1:1) were obviously observed with greatly improved signal-to-noise (S/N) ratio. Meanwhile, the enrichment results of non-fat milk and human serum also show the enrichment selectivity from complex biological samples. This study will provide a novel insight for selective enrichment of glycopeptides and phosphopeptides in post-translational modification proteomics research.