Protein chemical synthesis by serine and threonine ligation

被引：221

作者：

Zhang, Yinfeng ^{[1
]}

Xu, Ci ^{[1
]}

Lam, Hiu Yung ^{[1
]}

Lee, Chi Lung ^{[1
]}

Li, Xuechen ^{[1
]}

机构：

[1] Univ Hong Kong, Dept Chem, Hong Kong, Hong Kong, Peoples R China

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2013年 / 110卷 / 17期

关键词：

synthetic protein; acyl transfer; chemoselective ligation; PRIOR THIOL CAPTURE; INTRAMOLECULAR O; N-ACYL TRANSFER; PEPTIDE-BOND FORMATION; STAUDINGER LIGATION; SIDE-CHAIN; CYSTEINE; ACYLPHOSPHATASE; STRATEGIES; THIOESTER; MECHANISM;

D O I：

10.1073/pnas.1221012110

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：6657 / 6662

页数：6