Antos John M, Francis Matthew B
Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA.
Curr Opin Chem Biol. 2006 Jun;10(3):253-62. doi: 10.1016/j.cbpa.2006.04.009. Epub 2006 May 12.
The broad utility of protein bioconjugates has created a need for new and diverse strategies for site-selective protein modification. In particular, chemical reactions that target alternative amino acid side chains or unnatural functional groups are emerging as a valuable complement to more commonly used lysine- and cysteine-based strategies. Considering their widespread use in organic synthesis, reactions catalyzed by transition metals could provide a particularly powerful set of transformations for the continued expansion of the bioconjugation toolkit. Recent efforts to apply transition metal catalysis to protein modification have resulted in new methods for protein cross-linking, tryptophan modification, tyrosine modification, reductive amination of protein amines, and unnatural amino acid labeling. These strategies have substantially expanded the synthetic flexibility of protein modification, and thus the range of applications for which bioconjugates can be used in chemical biology and materials science.
蛋白质生物共轭物的广泛应用催生了对位点选择性蛋白质修饰新的多样策略的需求。特别是，针对其他氨基酸侧链或非天然官能团的化学反应正成为常用的基于赖氨酸和半胱氨酸策略的宝贵补充。鉴于过渡金属催化在有机合成中的广泛应用，其催化的反应可为生物共轭工具集的持续扩展提供一套特别强大的转化方法。最近将过渡金属催化应用于蛋白质修饰的努力已产生了蛋白质交联、色氨酸修饰、酪氨酸修饰、蛋白质胺的还原胺化以及非天然氨基酸标记的新方法。这些策略极大地扩展了蛋白质修饰的合成灵活性，从而扩大了生物共轭物在化学生物学和材料科学中的应用范围。
