Studies on Peptides. CXLVIII. Application of a New Deprotecting Procedure with Trimethylsilyl Trifluoromethanesulfonate for the Syntheses of Two Porcine Spinal Cord Peptides, Neuromedin U-8 and Neuromedin U-25

NOBUTAKA FUJII; OSAMU IKEMURA; SUSUMU FUNAKOSHI; HISAYUKI MATSUO; TOMIO SEGAWA; YOSHIHIRO NAKATA; ATSUKO INOUE; HARUAKI YAJIMA

doi:10.1248/cpb.35.1076

NOBUTAKA FUJII, OSAMU IKEMURA, SUSUMU FUNAKOSHI, HISAYUKI MATSUO, TOMIO SEGAWA, YOSHIHIRO NAKATA, ATSUKO INOUE, HARUAKI YAJIMA

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Keywords: porcine spinal cord peptide, neuromedin U-8, neuromedin U-25, thioanisolemediated deprotection, trifluoromethanesulfonic acid deprotection, deprotecting reagent, trimethylsilyl trifluoromethanesulfonate, uterus contractile activity

JOURNAL FREE ACCESS

1987 Volume 35 Issue 3 Pages 1076-1084

DOI https://doi.org/10.1248/cpb.35.1076

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Abstract

The usefulness of a new deprotecting procedure was demonstrated in the solution syntheses of two porcine spinal cord peptides, designated neuromedin U-8 and neuromedin U-25. Protected neuromedin U-8 (8-residue peptide), prepared by condensation of two fragments, served as a C-terminal amino component for the synthesis of neuromedin U-25 (25-residue peptide). Onto this fragment, five peptide fragments were successively condensed by the azide procedure to construct the entire amino acid sequence of neuromedin U-25, a possible biosynthetic precursor of neuromedin U-8. All protecting groups were cleaved from protected neuromedin U-8 and neuromedin U-25 by 1 M trimethylsilyl trifluoromethanesulfonate-thioanisole in trifluoroacetic acid. The results were compared with those obtained by trifluoromethanesulfonic acid deprotection. In terms of contractile activity in rat uterus, neuromedin U-25 was twice as active as neuromedin U-8.

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