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Protein chemical synthesis by serine and threonine ligation.

ABSTRACT: 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 (?11 kDa). The requisite peptide salicylaldehyde ester precursor is prepared in an epimerization-free manner via Fmoc-solid-phase peptide synthesis.

SUBMITTER: Zhang Y

PROVIDER: S-EPMC3637748 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Protein chemical synthesis by serine and threonine ligation.

Zhang Yinfeng Y Xu Ci C Lam Hiu Yung HY Lee Chi Lung CL Li Xuechen X

Proceedings of the National Academy of Sciences of the United States of America 20130408 17

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 (∼11 kDa). The requisite peptide salicylaldehyde ester precursor is prepared in an epimerization-free manner via Fmoc-solid-phase p ...[more]

PMID: 23569249

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