Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 7, Issue 9, Pages 474-487Publisher
WILEY
DOI: 10.1002/psc.341
Keywords
expressed peptide; Max protein; peptide synthesis; peptide building block; peptide thioester; phosphorylated peptide; transamination
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An expressed peptide proved to be useful as a building block for the synthesis of a polypeptide via the thioester method. A partially protected peptide segment, for use as a C-terminal building block. could be prepared from a recombinant protein: its N-terminal amino acid residue was transaminated to an alpha -oxoacyl group, the side-chain amino groups were then protected with t-butoxycarbonyl (Boc) groups, and, finally, the alpha -oxoacyl group was removed. On the other hand, an O-phosphoserine-containing peptide thioester was synthesized via a solid-phase method using Boc chemistry. These building blocks were then condensed in the presence of silver ions and an active ester component. During the condensation, epimerization at the condensation site could be suppressed by the use of N,N-dimthylformamide (DMF) as a solvent. Using this strategy, a phosphorylated partial peptide of the p21Max protein, [Ser(PO3H2)(2.11)]-p21Max(1 - 101), was successfully synthesized. Copyright (C) 2001 European Peptide Society and John Wiley & Sons. Ltd.
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