Conformation of D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2 (CTP-NH2), a highly selective mu-opioid antagonist peptide, by 1H and 13C n.m.r.

J. T. Pelton, M. Whalon, W. L. Cody, Victor J Hruby

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The 1H and 13C n.m.r. spectral parameters of CTP-NH2 [D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2], a potent, highly selective μ-opiate antagonist, were measured in aqueous solution and a possible conformation has been deduced from the spectral data. The data are consistent with a type II' β-turn for the tetrapeptide sequence -Tyr3-D-Trp4-Lys5-Thr6-. Solvent shielding of the Cys2 amide proton, observed in variable temperature experiments, suggestsan orientation of this amide proton toward the gem dimethyls of Pen7 with possible hydrogen bonding to the Thr6 carbonyl oxygen, and a dihedral angle of -110° for the disulfide bond. Partially relaxed Fourier transform 13C relaxation studies confirm a constrained cyclic system, with the Cα carbons in the 'hinge' of the β-turn having the shortest t1 times. Segmental motion was observed for the side chain of Lys5.

Original languageEnglish (US)
Pages (from-to)109-115
Number of pages7
JournalInternational Journal of Peptide and Protein Research
Volume31
Issue number2
StatePublished - 1988

Fingerprint

Opioid Peptides
Narcotic Antagonists
Amides
Conformations
Protons
Opiate Alkaloids
Gems
Fourier Analysis
Dihedral angle
Hinges
Hydrogen Bonding
Disulfides
Shielding
Fourier transforms
Hydrogen bonds
Carbon
Oxygen
Temperature
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{a6040462745c492c9fb4afa9afcc471f,
title = "Conformation of D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2 (CTP-NH2), a highly selective mu-opioid antagonist peptide, by 1H and 13C n.m.r.",
abstract = "The 1H and 13C n.m.r. spectral parameters of CTP-NH2 [D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2], a potent, highly selective μ-opiate antagonist, were measured in aqueous solution and a possible conformation has been deduced from the spectral data. The data are consistent with a type II' β-turn for the tetrapeptide sequence -Tyr3-D-Trp4-Lys5-Thr6-. Solvent shielding of the Cys2 amide proton, observed in variable temperature experiments, suggestsan orientation of this amide proton toward the gem dimethyls of Pen7 with possible hydrogen bonding to the Thr6 carbonyl oxygen, and a dihedral angle of -110° for the disulfide bond. Partially relaxed Fourier transform 13C relaxation studies confirm a constrained cyclic system, with the Cα carbons in the 'hinge' of the β-turn having the shortest t1 times. Segmental motion was observed for the side chain of Lys5.",
author = "Pelton, {J. T.} and M. Whalon and Cody, {W. L.} and Hruby, {Victor J}",
year = "1988",
language = "English (US)",
volume = "31",
pages = "109--115",
journal = "International Journal of Peptide and Protein Research",
issn = "0367-8377",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Conformation of D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2 (CTP-NH2), a highly selective mu-opioid antagonist peptide, by 1H and 13C n.m.r.

AU - Pelton, J. T.

AU - Whalon, M.

AU - Cody, W. L.

AU - Hruby, Victor J

PY - 1988

Y1 - 1988

N2 - The 1H and 13C n.m.r. spectral parameters of CTP-NH2 [D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2], a potent, highly selective μ-opiate antagonist, were measured in aqueous solution and a possible conformation has been deduced from the spectral data. The data are consistent with a type II' β-turn for the tetrapeptide sequence -Tyr3-D-Trp4-Lys5-Thr6-. Solvent shielding of the Cys2 amide proton, observed in variable temperature experiments, suggestsan orientation of this amide proton toward the gem dimethyls of Pen7 with possible hydrogen bonding to the Thr6 carbonyl oxygen, and a dihedral angle of -110° for the disulfide bond. Partially relaxed Fourier transform 13C relaxation studies confirm a constrained cyclic system, with the Cα carbons in the 'hinge' of the β-turn having the shortest t1 times. Segmental motion was observed for the side chain of Lys5.

AB - The 1H and 13C n.m.r. spectral parameters of CTP-NH2 [D-Phe-Cys-Tyr-D-Trp-Lys-Thr-Pen-Thr-NH2], a potent, highly selective μ-opiate antagonist, were measured in aqueous solution and a possible conformation has been deduced from the spectral data. The data are consistent with a type II' β-turn for the tetrapeptide sequence -Tyr3-D-Trp4-Lys5-Thr6-. Solvent shielding of the Cys2 amide proton, observed in variable temperature experiments, suggestsan orientation of this amide proton toward the gem dimethyls of Pen7 with possible hydrogen bonding to the Thr6 carbonyl oxygen, and a dihedral angle of -110° for the disulfide bond. Partially relaxed Fourier transform 13C relaxation studies confirm a constrained cyclic system, with the Cα carbons in the 'hinge' of the β-turn having the shortest t1 times. Segmental motion was observed for the side chain of Lys5.

UR - http://www.scopus.com/inward/record.url?scp=0023856908&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023856908&partnerID=8YFLogxK

M3 - Article

C2 - 2896638

AN - SCOPUS:0023856908

VL - 31

SP - 109

EP - 115

JO - International Journal of Peptide and Protein Research

JF - International Journal of Peptide and Protein Research

SN - 0367-8377

IS - 2

ER -