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The Membrane Mediated Conformation of Dynorphin A(1-13) as Studied by Transferred Nuclear Overhauser Effect Spectroscopy

Authors :
MCMASTER UNIV HAMILTON (ONTARIO)
VAN Gorkom, L. C.
Lancaster, C. R.
St-Pierre, S.
Bothner-By, A. A.
Epand, R. M.
MCMASTER UNIV HAMILTON (ONTARIO)
VAN Gorkom, L. C.
Lancaster, C. R.
St-Pierre, S.
Bothner-By, A. A.
Epand, R. M.
Source :
DTIC AND NTIS
Publication Year :
1992

Abstract

Dynorphin A is a potent opioid peptide with high specificity for the kappa-opioid receptor. The kappa-agonists are of clinical interest because kappa-receptors have been found to mediate analgesia with low addictive potential. The N-terminal fragment Dynorphin has high potency and kappa selectivity comparable to the natural 17 amino-acid peptide. The membrane is believed to play an important role in the receptor-peptide interactions. We report the conformational analysis of Dynorphin A at the surface of small uni-lamellar phosphatidylcholine vesicles.

Details

Database :
OAIster
Journal :
DTIC AND NTIS
Notes :
text/html, English
Publication Type :
Electronic Resource
Accession number :
edsoai.ocn831630790
Document Type :
Electronic Resource