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Structure and Activity of (2,8)-Dicarba-(3,12)-cystino α-ImI, an α-Conotoxin Containing a Nonreducible Cystine Analogue†

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The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville 3050, Victoria, Australia, School of Chemistry, Monash University, Clayton 3800, Victoria, Australia, Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne, Parkville 3010, Australia, Faculty of Pharmacy, The University of Sydney, Sydney, NSW 2006, Australia
†Assigned chemical shifts, experimental restraints and structures have been deposited with the BioMagResBank database with accession number 20033.
* To whom correspondence should be addressed. Phone: +61 3 9345 2306. Fax: +61 3 9345 2686. E-mail: [email protected]
‡The Walter & Eliza Hall Institute of Medical Research.
§Monash University.
∥University of Melbourne.
⊥University of Sydney.
Cite this: J. Med. Chem. 2009, 52, 3, 755–762
Publication Date (Web):January 6, 2009
https://doi.org/10.1021/jm8011504
Copyright © 2009 American Chemical Society
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    Abstract

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    The α-conotoxins are potent and selective antagonists of nicotinic acetylcholine receptors (nAChR). Exploitation of these and other peptides in research and clinical settings has been hampered by the lability of the disulfide bridges that are essential for toxin structure and activity. One solution to this problem is replacement of cystine bridges with nonreducible dicarba linkages. We explore this approach by determining the solution structure and functional characteristics of a dicarba analogue of the α-conotoxin α-ImI, (2,8)-dicarba-(3,12)-cystino α-ImI. The structure of the dicarba analogue was similar to that of native α-ImI, with differences attributable to the different covalent geometry of the disulfide and dicarba bridges. Dicarba-α-ImI maintained inhibitory activity of nAChR comparable to that of native α-ImI in two in vitro assays. These findings confirm the potential of the dicarba linkage to improve stability while maintaining α-conotoxin function.

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    Two tables containing assigned chemical shifts and amide temperature coefficients for dicarba-ImI, and seven figures showing the dose response of α-ImI and dicarba-ImI on nicotine-evoked adrenaline release from bovine adrenal chromaffin cells, 1H NMR spectra of dicarba α-ImI isomer I and II, a NOESY spectrum showing exchange-derived cross peaks involving alternate conformational states of isomer II, 1H 1D and DQF-COSY spectra of isomer II showing strong 3JHγ−Hγ coupling across the dicarba bridge, representative NOESY and TOCSY spectra of isomer I and the ensemble of 20 structures determined for dicarba α-ImI. This material is available free of charge via the Internet at http://pubs.acs.org.

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