His-Tagging:探索对含组氨酸生物活性肽序列的精确化学修饰

IF 1.7 4区 化学 Q3 CHEMISTRY, ORGANIC
Synlett Pub Date : 2024-06-03 DOI:10.1055/s-0043-1775364
Sourav Chatterjee, Bishwajit Paul, Govindaswamy Shanker
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引用次数: 0

摘要

生物大分子(尤其是肽类)的修饰已引起研究人员的极大关注,它实际上是化学与生物学之间的纽带。肽的修饰可以促进肽药物、抗体药物共轭物和分子成像探针等的生成。在此,我们精心整理了含有组氨酸的生物活性肽序列的反应和化学转化,这些反应和化学转化有利于生物应用。本报告还重点介绍了组氨酸化学修饰的策略,这些策略可能会激发多肽研究人员和合成化学家的想象力。1 引言 2 生物活性肽和蛋白质中的组氨酸修饰 3 组氨酸邻位的远程生物活性肽和蛋白质修饰 4 结论和未来方向
本文章由计算机程序翻译,如有差异,请以英文原文为准。

His-Tagging: Exploring Precise Chemical Modification of Histidine-Containing Bioactive Peptide Sequences

His-Tagging: Exploring Precise Chemical Modification of Histidine-Containing Bioactive Peptide Sequences

The modification of biomolecules, particularly peptides, has garnered considerable attention from researchers, effectively serving as a connection between chemistry and biology. The modification of peptides can facilitate, among others, the generation of peptide drugs, antibody–drug conjugates, and probes for molecular imaging. Herein, we have carefully curated reactions and chemical transformations of bioactive peptide sequences equipped with histidine amino acids that are conducive for biological applications. This Account also highlights strategies for the chemical modification of histidine that might capture the imagination of both peptide researchers and synthetic chemists.

1 Introduction

2 Histidine Modification in Bioactive Peptides and Proteins

3 Remote Bioactive Peptides and Protein Modification Adjacent to Histidine

4 Conclusions and Future Directions

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来源期刊
Synlett
Synlett 化学-有机化学
CiteScore
3.40
自引率
5.00%
发文量
369
审稿时长
1 months
期刊介绍: SYNLETT is an international journal reporting research results and current trends in chemical synthesis in short personalized reviews and preliminary communications. It covers all fields of scientific endeavor that involve organic synthesis, including catalysis, organometallic, medicinal, biological, and photochemistry, but also related disciplines and offers the possibility to publish scientific primary data.
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