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Biophysical Journal 86:1587-1600 (2004)
© 2004 The Biophysical Society

A Multidimensional 1H NMR Investigation of the Conformation of Methionine-Enkephalin in Fast-Tumbling Bicelles

Isabelle Marcotte *, Frances Separovic {dagger}, Michèle Auger * and Stéphane M. Gagné {ddagger}

* Département de Chimie, Centre de Recherche en Sciences et Ingénierie des Macromolécules, Université Laval, Québec, Québec, Canada, G1K 7P4; {dagger} School of Chemistry, University of Melbourne, VIC 3010, Australia; and {ddagger} Département de Biochimie et Microbiologie, Centre de Recherche sur la Fonction, la Structure et l'Ingénierie des Protéines, Université Laval, Québec, Québec, Canada, G1K 7P4

Correspondence: Address reprint requests to Michèle Auger, Département de Chimie, CERSIM, Université Laval, Québec, Québec, Canada, G1K 7P4. Tel.: 418-656-3393; Fax: 418-656-7916; E-mail: michele.auger{at}chm.ulaval.ca.

Enkephalins are pentapeptides found in the central nervous system. It is believed that these neuropeptides interact with the nerve cell membrane to adopt a conformation suitable for their binding to an opiate receptor. In this work, we have determined the three-dimensional structure of methionine-enkephalin (Menk) in fast-tumbling bicelles using multidimensional 1H NMR. Bicelles were selected as model membranes because both their bilayer organization and composition resemble those of natural biomembranes. The effect of the membrane composition on the peptide conformation was explored using both zwitterionic (PC bicelles) and negatively charged bicelles (Bic/PG). Pulsed field gradient experiments allowed the determination of the proportion of Menk bound to the model membranes. Approximately 60% of the water-soluble enkephalin was found to associate to the bicellar systems. Structure calculations from torsion angle and NOE-based distance constraints suggest the presence of both µ- and {delta}-selective conformers of Menk in each system and slightly different conformers in PC bicelles and Bic/PG. As opposed to previous studies of enkephalins in membrane mimetic systems, our results show that these opiate peptides could adopt several conformations in a membrane environment, which is consistent with the flexibility and poor selectivity of enkephalins.




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