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Relative conformational rigidity in oxytocin and (1-penicillamine)-oxytocin: a proposal for the relationship of conformational flexibility to peptide hormone agonism and antagonism.
Author(s) -
Jean Paul Meraldi,
Victor J. Hruby,
Anne I. Brewster
Publication year - 1977
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.4.1373
Subject(s) - oxytocin , antagonism , agonism , penicillamine , chemistry , peptide , hormone , stereochemistry , receptor , pharmacology , endocrinology , biochemistry , biology , organic chemistry , politics , political science , law
A comparative study of the proton and carbon-13 nuclear magnetic resonance spectral parameters of the peptide hormone oxytocin and of its competitive inhibitor [1-L-penicillamine]oxytocin has been made, and the results analyzed in terms of comparative conformational and dynamic properties. The results indicate that oxytocin has a flexible conformation, while [1-L-penicillamine]oxytocin has a more restricted conformation. The results provide a framework for understanding the mechanism of peptide hormone agonism and antagonism for these compounds, and an approach for understanding some features of the interaction of the hormone and related compounds with their receptor.

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