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

doi:10.1111/j.1399-3011.1987.tb03363.x

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

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

4 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 ³J_NH‐cα_H 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 language	English (US)
Pages (from-to)	541-547
Number of pages	7
Journal	International journal of peptide and protein research
Volume	30
Issue number	4
DOIs	https://doi.org/10.1111/j.1399-3011.1987.tb03363.x
State	Published - Oct 1987

Keywords

1H‐n.m.r
conformation
somatostatin analogue

ASJC Scopus subject areas

Biochemistry

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10.1111/j.1399-3011.1987.tb03363.x

Cite this

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

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.",

keywords = "1H‐n.m.r, conformation, somatostatin analogue",

author = "C. WYNANTS and E. SUGG and HRUBY, \{V. J.\} and \{VAN BINST\}, G.",

year = "1987",

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doi = "10.1111/j.1399-3011.1987.tb03363.x",

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journal = "International journal of peptide and protein research",

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T1 - Conformational study of a somatostatin analogue by high‐field n.m.r. spectroscopy, in aqueous solution

AU - WYNANTS, C.

AU - SUGG, E.

AU - HRUBY, V. J.

AU - VAN BINST, G.

PY - 1987/10

Y1 - 1987/10

N2 - 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.

AB - 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.

KW - 1H‐n.m.r

KW - conformation

KW - somatostatin analogue

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

Abstract

Keywords

ASJC Scopus subject areas

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