Recent advances in protein modifications techniques for the targeting N-terminal cysteine,Peptide Science

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Recent advances in protein modifications techniques for the targeting N-terminal cysteine
Peptide Science ( IF 1.5 ) Pub Date : 2021-06-11 , DOI: 10.1002/pep2.24235
Nicholas Asiimwe _{1,

2} , Mohammad Faysal Al Mazid _{2,

3} , Dhiraj P. Murale ₄ , Yun Kyung Kim _{1,

2} , Jun‐Seok Lee ₅

Affiliation

N-terminal modifications of proteins have garnered the attention of chemical biologists because of their critical roles in numerous cellular processes, including protein translocation, protein structural and metabolic stability, and the regulation of the half-life of proteins by a process known as “N-end rule pathway.” In addition, other posttranslational modification processes also depend on the N-terminal signal sequences. Chemical probes are powerful tools that can be used to investigate N-terminal modifications, to gain structural and functional insights into protein modification, protein-protein interactions, protein localization, and protein dynamics. Most modifications target cysteine and lysine residues because of their high nucleophilicity. However, due to multiple occurrences of these residues in a protein at a given time, regioselective labeling can be quite difficult to accomplish. N-terminal cysteine presents itself as a unique practical option to overcome regioselectivity and site-specificity challenges. This review provides an overview of N-terminal cysteine labeling tools, including N-terminal cysteine condensation with aldehydes, cyanobenzothiazoles, cyclopropenones, and trans-thioesterification. The review also highlights the technical challenges of each of the techniques, which need to be addressed to broaden the scope of these approaches.

中文翻译：

靶向 N 端半胱氨酸的蛋白质修饰技术的最新进展

蛋白质的 N 端修饰引起了化学生物学家的关注，因为它们在许多细胞过程中发挥着关键作用，包括蛋白质易位、蛋白质结构和代谢稳定性，以及通过称为“N”的过程调节蛋白质的半衰期。 ——终结规则途径。” 此外，其他翻译后修饰过程也依赖于 N 端信号序列。化学探针是强大的工具，可用于研究 N 端修饰，以获得对蛋白质修饰、蛋白质-蛋白质相互作用、蛋白质定位和蛋白质动力学的结构和功能见解。大多数修饰针对半胱氨酸和赖氨酸残基，因为它们具有高亲核性。然而，由于在给定时间蛋白质中这些残基多次出现，区域选择性标记可能很难完成。N-末端半胱氨酸作为一种独特的实用选择来克服区域选择性和位点特异性挑战。本综述概述了 N 端半胱氨酸标记工具，包括 N 端半胱氨酸与醛缩合、氰基苯并噻唑、环丙烯酮和反式硫酯化。该审查还强调了每种技术的技术挑战，需要解决这些挑战以扩大这些方法的范围。氰基苯并噻唑、环丙烯酮和反式硫酯化。该审查还强调了每种技术的技术挑战，需要解决这些挑战以扩大这些方法的范围。氰基苯并噻唑、环丙烯酮和反式硫酯化。该审查还强调了每种技术的技术挑战，需要解决这些挑战以扩大这些方法的范围。

更新日期：2021-06-11

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