无痕合成蛋白硫酯：酶介导的肼解作用及随后半胱氨酸脯氨酸序列的自我编辑。
Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of the cysteinyl prolyl sequence.
机构信息
Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University, Tokushima 770-8505, Japan.
Institute of Medicinal Resources, Graduate School of Pharmaceutical Sciences, Tokushima University, Tokushima 770-8505, Japan.
出版信息
Chem Commun (Camb). 2019 Jun 21;55(49):7029-7032. doi: 10.1039/c9cc03583d. Epub 2019 May 29.
A traceless thioester-producing protocol featuring carboxypeptidase Y-mediated hydrazinolysis of cysteinyl prolyl leucine-tagged peptides has been developed. The hydrazinolysis followed by thioesterification affords cysteinyl prolyl thioesters. Self-editing of the tag and subsequent trans-thioesterification yields peptide thioesters. The developed protocol was successfully applied to the conversion of recombinant proteins to thioesters.
已开发出一种无痕硫酯生成方案，其特征在于通过羧肽酶 Y 介导的半胱氨酰脯氨酰亮氨酸标记肽的肼解反应。肼解反应后进行硫酯化反应可得到半胱氨酰脯氨酰硫酯。标签的自我编辑和随后的硫酯交换反应生成肽硫酯。该方案已成功应用于重组蛋白向硫酯的转化。
Zotero 插件