Hollow MnFe2O4@C@APBA Nanospheres with Size Exclusion and pH Response for Efficient Enrichment of Endogenous Glycopeptides

Hollow MnFe2O4@C@APBA Nanospheres with Size Exclusion and pH Response for Efficient Enrichment of Endogenous Glycopeptides
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具有尺寸排阻和 pH 响应的中空 MnFe2O4@C@APBA 纳米球可有效富集内源糖肽

DOI:
10.1021/acsami.0c22221
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发表时间:
2021
影响因子:
9.5
通讯作者:
Teng Guixiang
Teng Guixiang
中科院分区:
材料科学2区
文献类型:
--
作者:
Zhang Chun;Jin Xiaodong;Wang Liping;Jin Chengzhao;Han Xiaoqian;Ma Weigang;Li Xingang;Teng Guixiang

文献摘要

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糖肽的富集和检测是临床诊断复杂疾病的重要手段。富集材料在此过程中起着关键作用,它们必须具有有效的样品筛选能力,以消除非糖肽的干扰。本工作制备了具有磁性和pH响应性的新型中空MnFe2O4@C@APBA纳米球(HMCAs),用于糖肽的富集。所制备的复合材料具有合适的中空结构和较大的比表面积,且其空腔中的硼羟基在不同pH下可固定或断开糖肽的亲水基团,从而实现糖肽的可控吸附或脱附。富集结果表明,HMCAs具有良好的富集性能:检测限极低(约0.5 fmol μL-1)、良好的体积排阻效应(HRP/BSA,1:800,w/w)、良好的普适性(HRP、IgG和RNase B)和较高的结合容量(150 mg/g)。为了验证该材料在实际中的应用,将HMCAs用于复杂样品的分析,发现在2 μL人血清的三次重复分析中,从210种糖蛋白中鉴定出474种糖肽。结果表明,HMCAs可作为一种很有前途的富集材料,用于基于MS的糖蛋白质组学及相关领域的糖肽表征。
Enrichment and detection of glycopeptides are an important clinical measure for the diagnosis of complex diseases. Enrichment materials play a key role in this process; they must have an effective sample-screening ability to eliminate the interference of nonglycopeptides. In this work, novel hollow MnFe2O4@C@APBA nanospheres (HMCAs) with magnetic and pH responsiveness were prepared for glycopeptide enrichment. The as-prepared composites have a suitable hollow structure and large specific surface area, and the boron hydroxyl group in their cavities can fix or disconnect the hydrophilic groups of the glycopeptides at different pH, so the glycopeptides can be adsorbed or desorbed in a controllable way. Enrichment results showed that the HMCAs exhibited an excellent enrichment performance: ultralow limit of detection (approximately 0.5 fmol μL–1), perfect size-exclusion effect (HRP/BSA, 1:800, w/w), favorable universality (HRP, IgG, and RNase B), and high binding capacity (150 mg/g). In order to verify the application of materials in practice, the HMCAs were used for the analysis of complex samples and it was found that 474 glycopeptides were identified from 210 glycoproteins in three replicate analyses of 2 μL of human serum. The results showed that the HMCAs could be used as a promising enrichment material for glycopeptide characterization in MS-based glycoproteomics and related fields.