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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acid Anhydride Hydrolases / chemical synthesis*
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Acylphosphatase
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Aldehydes / chemistry*
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Animals
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Chromatography, High Pressure Liquid
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Corticotropin-Releasing Hormone / chemical synthesis*
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Humans
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Mass Spectrometry
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Molecular Structure
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Peptides / chemistry*
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Protein Engineering / methods*
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Serine / chemistry
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Sheep
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Teriparatide / chemical synthesis*
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Threonine / chemistry
Substances
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Aldehydes
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Peptides
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Teriparatide
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salicylaldehyde
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Threonine
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Serine
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Corticotropin-Releasing Hormone
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Acid Anhydride Hydrolases