Abstract
Canine gastrin-releasing polypeptide (cGRP, characterized as a bombesin-like 27-residue peptide) was synthesized by successive azide condensations of 7 peptide fragments of established purity, followed by deprotection with trifluoromethanesulfonic acid in trifluoroacetic acid. Prior to deprotection, the Met(O) residue in the protected cGRP was reduced by brief treatment with phenylthiotrimethylsilane in the presence of a catalytic amount of trimethylsilyl trifluoromethanesulfonate. The homogeneous HPLC-purified product induced a significant increase of immunoreactive gastrin level in rat plasma, like synthetic human GRP.
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