Studies on Peptides. CLIV. Synthesis of a 36-Residue Peptide Amide Corresponding to the Entire Amino Acid Sequence of Human Pancreatic Polypeptide

NAOKI SUGIYAMA; NOBUTAKA FUJII; SUSUMU FUNAKOSHI; AKIHIRO FUNAKOSHI; KYOKO MIYASAKA; MITSURU AONO; MOTOYUKI MORIGA; KAZUTOMO INOUE; MASAFUMI KOGIRE; SHOICHIRO SUMI; RYUICHIRO DOI; TAKAYOSHI TOBE; HARUAKI YAJIMA

doi:10.1248/cpb.35.3585

NAOKI SUGIYAMA, NOBUTAKA FUJII, SUSUMU FUNAKOSHI, AKIHIRO FUNAKOSHI, KYOKO MIYASAKA, MITSURU AONO, MOTOYUKI MORIGA, KAZUTOMO INOUE, MASAFUMI KOGIRE, SHOICHIRO SUMI, RYUICHIRO DOI, TAKAYOSHI TOBE, HARUAKI YAJIMA

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Keywords: human pancreatic polypeptide synthesis, β-menthylaspartate, hard acid deprotection, trimethylsilyl trifluoromethanesulfonate, soft base, diphenylsulfide-mediated deprotection, inhibited pancreatic secretion

JOURNAL FREE ACCESS

1987 Volume 35 Issue 9 Pages 3585-3596

DOI https://doi.org/10.1248/cpb.35.3585

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Abstract

A 36-residue peptide corresponding to the entire amino acid sequence of human pancreatic polypeptide (hPP) was synthesized by the solution method. A new Asp derivative, Asp (OMen) [Men = menthyl] was employed. Seven fragments served to construct the peptide backbone of hPP and all the protecting groups employed were cleaved by 2 M trimethylsilyl trifluoromethane-sulfonate-diphenylsulfide/trifluoroacetic acid. The synthetic peptide inhibited protein secretion from rat pancreas.

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