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The Journal of Neuroscience, August 1, 1999, 19(15):6318-6326

Conformational Ensembles: The Role of Neuropeptide Structures in Receptor Binding

Arthur S. Edison, Eduardo Espinoza, and Cherian Zachariah

Department of Biochemistry and Molecular Biology, Center for Structural Biology, University of Florida Brain Institute, and National High Magnetic Field Laboratory, University of Florida, Gainesville, Florida 32610-0245

Conformational properties of several similar FMRFamide-like neuropeptides from mollusks were investigated by nuclear magnetic resonance (NMR) spectroscopy. It was found that amino acid substitutions in the N-terminal variable regions of the peptides had dramatic effects on the populations of reverse turns in solution. The populations of turns, as measured by two independent NMR parameters, were found to be highly correlated (r2 = 0.93 and 0.82) with IC50 values using receptor membrane preparations from Helix aspersa (Payza, 1987; Payza et al., 1989). These results suggest that the amount of turn in the free peptide can influence the receptor binding affinities of that peptide. On the basis of these observations, a model was developed in which only a single species from a conformational ensemble of an unbound peptide will bind to a particular receptor. Thus, the conformational ensemble reduces the effective concentration of a particular peptide with respect to a particular receptor.

Key words: FMRFamide-like peptides; NMR; structure-function relations; conformational averaging; dynamics; three-dimensional structure; reverse turn

Copyright © 1999 Society for Neuroscience  0270-6474/99/19156318-09$05.00/0


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