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

E. E. Sugg, D. Tourwe, W. Kazmierski, Victor J Hruby, G. Van Binst

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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
Publication statusPublished - 1988

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ASJC Scopus subject areas

  • Biochemistry

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