Protein chemical synthesis by serine and threonine ligation
Protein chemical synthesis by serine and threonine ligation
复制标题
DOI：
10.1073/pnas.1221012110
复制
发表时间：
2013-04-23
影响因子：
11.1
通讯作者：
Li, Xuechen
中科院分区：
文献类型：
--
作者：
Zhang, Yinfeng;Xu, Ci;Li, Xuechen
本研究建立了一种水杨醛酯介导的丝氨酸或苏氨酸残基连接法。这种肽连接方法的效用已被证明通过收敛合成的两种治疗肽-绵羊-corticoliberin和Forteo-和人红细胞酰基磷酸酶蛋白（类似于11 kDa）。必需的肽水杨醛酯前体通过Fmoc-固相肽合成以无差向异构化的方式制备。
An efficient method has been developed for the salicylaldehyde ester-mediated ligation of unprotected peptides at serine (Ser) or threonine (Thr) residues. The utility of this peptide ligation approach has been demonstrated through the convergent syntheses of two therapeutic peptides-ovine-corticoliberin and Forteo-and the human erythrocyte acylphosphatase protein (similar to 11 kDa). The requisite peptide salicylaldehyde ester precursor is prepared in an epimerization-free manner via Fmoc-solid-phase peptide synthesis.