New Opportunities and Challenges of Smart Polymers in Post-Translational Modification Proteomics
New Opportunities and Challenges of Smart Polymers in Post-Translational Modification Proteomics
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智能聚合物在翻译后修饰蛋白质组学中的新机遇和挑战
DOI：
10.1002/adma.201604670
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发表时间：
2017-05-24
影响因子：
29.4
通讯作者：
Sun, Taolei
中科院分区：
文献类型：
--
作者：
Qing, Guangyan;Lu, Qi;Sun, Taolei
蛋白质翻译后修饰(PTM)指的是蛋白质中各种官能团(如磷酸、多糖、甲基或泛素)的共价添加，显著增加了蛋白质的复杂性和多样性。PTMS在调节蛋白质功能和许多细胞过程中起着至关重要的作用。然而，在活的生物体中，天然的PTM蛋白通常以亚化学计量水平存在，这大大阻碍了基于质谱学的分析和鉴定。在过去的十年里，对PTM蛋白质组学深入研究的需求催生了各种选择性亲和材料，能够从高度复杂的生物样品中捕获微量的PTM多肽。然而，迫切需要新的设计思想或策略来满足日益复杂和准确的PTM蛋白质组学分析的要求，而传统的浓缩材料很难满足这一要求。考虑到蛋白质PTM的两种典型类型，即磷酸化和糖基化，本文综述了聚合物富集材料，重点介绍了智能聚合物基材料在智能模式下的优势。此外，还介绍了一些智能分离材料，展示了智能聚合物在PTM蛋白质组学中的诱人前景和挑战。
Protein post-translational modifications (PTMs), which denote covalent additions of various functional groups (e.g., phosphate, glycan, methyl, or ubiquitin) to proteins, significantly increase protein complexity and diversity. PTMs play crucial roles in the regulation of protein functions and numerous cellular processes. However, in a living organism, native PTM proteins are typically present at substoichiometric levels, considerably impeding mass-spectrometry-based analyses and identification. Over the past decade, the demand for in-depth PTM proteomics studies has spawned a variety of selective affinity materials capable of capturing trace amounts of PTM peptides from highly complex biosamples. However, novel design ideas or strategies are urgently required for fulfilling the increasingly complex and accurate requirements of PTM proteomics analysis, which can hardly be met by using conventional enrichment materials. Considering two typical types of protein PTMs, phosphorylation and glycosylation, an overview of polymeric enrichment materials is provided here, with an emphasis on the superiority of smart-polymer-based materials that can function in intelligent modes. Moreover, some smart separation materials are introduced to demonstrate the enticing prospects and the challenges of smart polymers applied in PTM proteomics.