Abstract
Human gastrin-releasing polypeptide (hGRP), which consists of 27 amino acid residues with a C-terminal amide, was synthesized by a conventional solution method, by assembling six peptide fragments followed by deprotection with 1M trifluoromethanesulfonic acid-thioanisole in trifluoroacetic acid. Met(O) employed was reduced by treatment with phenylthiotrimethylsilane in the presence of trimethylsilyl trifluoromethanesulfonate before deprotection. The synthetic peptide was as active as synthetic porcine GRP, in terms of immunoreactive gastrin release in rats.
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