Proton n.m.r. investigation of conformational influence of penicillamine residues on the disulfide ring system of opioid receptor selective Somatostatin derivatives

ELIZABETH E. SUGG, DIRK TOURWE, WIESLAW KAZMIERSKI, VICTOR J. HRUBY, GEORGES VAN BINST

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Three cyclic disulfide analogs related to somatostatin, d‐Phe1 ‐Cys2‐Tyr3‐d‐Trp4‐Lys5‐Thr6‐Xxx7‐Thr8NH2 (where Xxx =l‐Pen 1; l‐Cys 3; or d‐Pen 4) were examined in DMSO‐d6 by one‐ and two‐dimensional proton n.m.r. spectroscopy in order to analyze the conformational influence of the position‐7 residue on the 20‐membered disulfide ring. From these studies it was concluded that all three analogs maintain a β II turn solution conformation for the core tetrapeptide‐Tyr3‐d‐Trp4‐Lys5‐Thr6‐. However, the disulfide conformation differs in the analogs, with 1 and 3 having a left‐handed and 4 a right‐handed disulfide chirality.

Original languageEnglish (US)
Pages (from-to)192-200
Number of pages9
JournalInternational journal of peptide and protein research
Volume31
Issue number2
DOIs
StatePublished - Feb 1988

Keywords

  • conformation
  • cyclic peptide
  • somatostatin analogs
  • two‐dimensional n.m.r.

ASJC Scopus subject areas

  • Biochemistry

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