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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:
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.
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页码:6657 / 6662
页数:6
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