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

doi:10.1111/j.1399-3011.1988.tb00022.x

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	192-200
Number of pages	9
Journal	International journal of peptide and protein research
Volume	31
Issue number	2
DOIs	https://doi.org/10.1111/j.1399-3011.1988.tb00022.x
State	Published - Feb 1988
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biochemistry

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10.1111/j.1399-3011.1988.tb00022.x

Cite this

SUGG, ELIZABETH. E., TOURWE, DIRK., KAZMIERSKI, WIESLAW., HRUBY, VICTOR. J., & VAN BINST, GEORGES. (1988). Proton n.m.r. investigation of conformational influence of penicillamine residues on the disulfide ring system of opioid receptor selective Somatostatin derivatives. International journal of peptide and protein research, 31(2), 192-200. https://doi.org/10.1111/j.1399-3011.1988.tb00022.x

Proton n.m.r. investigation of conformational influence of penicillamine residues on the disulfide ring system of opioid receptor selective Somatostatin derivatives. / SUGG, ELIZABETH E.; TOURWE, DIRK; KAZMIERSKI, WIESLAW et al.
In: International journal of peptide and protein research, Vol. 31, No. 2, 02.1988, p. 192-200.

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

SUGG, ELIZABETHE, TOURWE, DIRK, KAZMIERSKI, WIESLAW, HRUBY, VICTORJ & VAN BINST, GEORGES 1988, 'Proton n.m.r. investigation of conformational influence of penicillamine residues on the disulfide ring system of opioid receptor selective Somatostatin derivatives', International journal of peptide and protein research, vol. 31, no. 2, pp. 192-200. https://doi.org/10.1111/j.1399-3011.1988.tb00022.x

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

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.",

keywords = "conformation, cyclic peptide, somatostatin analogs, two‐dimensional n.m.r.",

author = "SUGG, {ELIZABETH E.} and DIRK TOURWE and WIESLAW KAZMIERSKI and HRUBY, {VICTOR J.} and {VAN BINST}, GEORGES",

year = "1988",

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doi = "10.1111/j.1399-3011.1988.tb00022.x",

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AU - SUGG, ELIZABETH E.

AU - TOURWE, DIRK

AU - KAZMIERSKI, WIESLAW

AU - HRUBY, VICTOR J.

AU - VAN BINST, GEORGES

PY - 1988/2

Y1 - 1988/2

N2 - 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.

AB - 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.

KW - conformation

KW - cyclic peptide

KW - somatostatin analogs

KW - two‐dimensional n.m.r.

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

Abstract

Keywords

ASJC Scopus subject areas

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