Proteins are the most abundant biomolecules within a cell and are involved in all biochemical cellular processes, fulfilling specific functions with unmatched precision. This unique specificity makes proteins an ideal scaffold to generate tools for the exploration of natural systems or for the construction of modern therapeutics. Thus, the chemoselective modification of proteins with functionalities that are not defined by the genetic code has become an indispensable approach for life science research and the development of therapeutics. Amongst site-selective strategies for protein modification, cysteine-selective approaches have long been used for the generation of functional protein conjugates and new reactions continue to emerge, offering solutions for diverse research questions. In this review, we are highlighting new strategies for the chemoselective modification of cysteine residues in peptides, proteins and antibodies with a particular focus on the most recent years. We lay special focus on new reagents for efficient cysteine conjugation that produce stable conjugation products with significant pharmaceutical application.

中文翻译：

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硫醇选择性生物偶联反应的最新进展。

蛋白质是细胞内最丰富的生物分子，参与所有生化细胞过程，以无与伦比的精度完成特定功能。这种独特的特异性使蛋白质成为生成探索自然系统或构建现代疗法的工具的理想支架。因此，对具有遗传密码未定义的功能的蛋白质进行化学选择性修饰已成为生命科学研究和治疗学开发不可或缺的方法。在蛋白质修饰的位点选择性策略中，半胱氨酸选择性方法长期以来一直用于生成功能性蛋白质偶联物，并且新反应不断出现，为各种研究问题提供了解决方案。在这次审查中，我们正在重点介绍肽、蛋白质和抗体中半胱氨酸残基化学选择性修饰的新策略，尤其是最近几年。我们特别关注用于高效半胱氨酸偶联的新试剂，这些试剂可产生具有重要药物应用的稳定偶联产物。