Division of Physical Biochemistry, MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA.
Biopolymers. 2010;94(4):530-41. doi: 10.1002/bip.21455.
Native chemical ligation (NCL) is a simple procedure that enables synthetic access to many proteins and is increasingly harnessed to study protein structure and function. However, the generality of this method is limited by the requirement for cysteine residues suitably positioned throughout the target protein. Auxiliary approaches have been developed to overcome this limitation, wherein a removable group is introduced at the amino terminus of a peptide conveying ligation properties comparable to cysteine. Present auxiliary approaches combine the thioester exchange concept applied first in NCL with a number of acyl transfer reactions first systematically explored by Kemp and coworkers. The current methods for auxiliary mediated ligation appear promising for the synthesis of proteins and in particular post-translational modified proteins.
天然化学连接（NCL）是一种简单的方法，可用于合成许多蛋白质，并越来越多地用于研究蛋白质结构和功能。然而，该方法的通用性受到限制，因为需要在目标蛋白质中适当位置的半胱氨酸残基。已经开发了辅助方法来克服此限制，其中在肽的氨基末端引入可移动基团，该肽传递与半胱氨酸相当的连接性质。当前的辅助方法将首先在 NCL 中应用的硫酯交换概念与 Kemp 及其同事首先系统地探索的多种酰基转移反应结合在一起。用于辅助介导连接的当前方法似乎很有希望用于蛋白质的合成，尤其是翻译后修饰的蛋白质的合成。
