Conformational study of a somatostatin analogue by high‐field n.m.r. spectroscopy, in aqueous solution

C. WYNANTS, E. SUGG, V. J. HRUBY, G. VAN BINST

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The cyclic analogue of somatostatin (SRIF), D‐Phe‐Cys‐Tyr‐D‐Trp‐Lys‐Thr‐Cys‐Thr‐NH2 (CTC), exhibits good affinity for both opioid and SRIF receptor systems. Its conformational properties were examined in water by high‐field proton n.m.r. spectroscopy and compared with results previously obtained with structurally related analogues SMS 201–995 and Sandoz 204–090 in the same solvent. The assignments were made using 2 D‐n.m.r. methods, especially long‐range connectivities between neighbouring α protons, and between β and aromatic protons. The 3JNH‐cαH and Δδ/ΔT values are compatible with an equilibrium between two γ turns involving residues 2, 3 and 4 and residues 3, 4, and 5, respectively.

Original languageEnglish (US)
Pages (from-to)541-547
Number of pages7
JournalInternational journal of peptide and protein research
Volume30
Issue number4
DOIs
StatePublished - Oct 1987

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Keywords

  • 1H‐n.m.r
  • conformation
  • somatostatin analogue

ASJC Scopus subject areas

  • Biochemistry

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