Abstract：
The demand for creation of protein diversity and regulation of protein function through native protein modification and post-translational modification has ignited the development of selective chemical modification methods for peptides and proteins. Chemical bioconjugation offers selective functionalization providing bioconjugates with desired properties and functions for diverse applications in chemical biology, medicine, and biomaterials. The amino group existing at the lysine residue and N-terminus of peptides and proteins has been extensively studied in bioconjugation because of its good nucleophilicity and high surface exposure. Herein, we review the development of chemical methods for modification of the amino groups on lysine residue and N-terminus featuring excellent selectivity, mild reaction conditions, short reaction time, high conversion, biocompatibility, and preservation of protein integrity. This review is organized based on the chemoselectivity and site-selectivity of the chemical bioconjugation reagents to the amino acid residues aiming to provide guidance for the selection of appropriate bioconjugation methods.
摘要：
通过天然蛋白质修饰和翻译后修饰来产生蛋白质多样性和调节蛋白质功能的需求已经引发了用于肽和蛋白质的选择性化学修饰方法的发展。化学生物缀合提供选择性官能化，为化学生物学中的各种应用提供具有所需特性和功能的生物缀合物。医学,和生物材料。肽和蛋白质的赖氨酸残基和N末端存在的氨基由于其良好的亲核性和高的表面暴露而在生物缀合中被广泛研究。在这里，我们回顾了修饰赖氨酸残基和N末端氨基的化学方法的发展，这些方法具有优异的选择性，温和的反应条件，短反应时间,高转化率,生物相容性，和保持蛋白质的完整性。这篇综述是基于化学生物缀合试剂对氨基酸残基的化学选择性和位点选择性组织的，旨在为选择合适的生物缀合方法提供指导。
