SYNTHESIS OF PROTECTED SECRETIN16–27 ON A MERRIFIELD RESIN

DAVID E. WRIGH, NIRANKAR S. AGARWAL, VICTOR J. HRUBY

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

The partially protected dodecapeptide to secretin, H ‐ Ser(Bzl) ‐ Ala ‐ Arg(Tos) ‐ Leu ‐ Gln ‐ Arg(Tos) ‐ Leu ‐ Leu ‐ Gln ‐ Gly ‐ Leu ‐ Val ‐ NH2 (protected secretin16–27) was prepared using a standard Merrifield resin and solid phase synthesis methods. For comparative purposes the unprotected peptide also was prepared on a benzhydrylamine resin. Contrary to previous reports, the valine C‐terminal peptide can be cleaved from the resin and the amide obtained in high yield. A variety of conditions were examined to accomplish the cleavage of the peptide from the resin in its carboxamide terminal form. The best conditions found were transesterification followed by ammonolysis in a mixed solvent system. A thin‐layer chromatography system which clearly separates the methyl ester and carboxamide terminal secretin16–27 was developed.

Original languageEnglish (US)
Pages (from-to)271-278
Number of pages8
JournalInternational journal of peptide and protein research
Volume15
Issue number3
DOIs
StatePublished - Mar 1980

Keywords

  • ammonolysis
  • benzhydrylamine resin
  • secretin
  • solid phase synthesis
  • transesterification

ASJC Scopus subject areas

  • Biochemistry

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