Soellner Matthew B, Dickson Kimberly A, Nilsson Bradley L, Raines Ronald T
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
J Am Chem Soc. 2003 Oct 1;125(39):11790-1. doi: 10.1021/ja036712h.
The Staudinger ligation between an azido-protein and a phosphinothioester-derivatized surface is demonstrated to be an effective means for the site-specific, covalent immobilization of a protein. Immobilization yields of >50% are obtained in <1 min, and immobilized proteins have >80% of their expected activity. No other method enables more rapid immobilization or a higher yield of active protein. Because azido-peptides and azido-proteins are readily attainable by synthesis, biosynthesis, or semisynthesis, the Staudinger ligation could be of unsurpassed utility in creating microarrays of functional peptides and proteins.
叠氮基蛋白质与硫代膦酸酯衍生化表面之间的施陶丁格连接被证明是一种用于蛋白质位点特异性共价固定的有效方法。在不到1分钟的时间内即可获得大于50%的固定产率，且固定后的蛋白质具有其预期活性的80%以上。没有其他方法能实现更快速的固定或更高产率的活性蛋白质。由于叠氮基肽和叠氮基蛋白质可通过合成、生物合成或半合成轻松获得，施陶丁格连接在创建功能性肽和蛋白质微阵列方面可能具有无与伦比的实用性。
