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
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
收藏
页码:6657 / 6662
页数:6
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