The synthesis and structure of an n-terminal dodecanoic acid conjugate of α-conotoxin MII

RIS ID

106080

Publication Details

Blanchfield, J., Dutton, J., Hogg, R., Craik, D., Adams, D., Lewis, R., Alewood, P. & Toth, I. (2001). The synthesis and structure of an n-terminal dodecanoic acid conjugate of α-conotoxin MII. Letters in Peptide Science, 8 (3-5), 235-239. Letters in Peptide Science

Abstract

The α-conotoxin MII is a 16 amino acid long peptide toxin isolated from the marine snail, Conus magus. This toxin has been found to be a highly selective and potent inhibitor of neuronal nicotinic acetylcholine receptors of the subtype α3β2. To improve the bioavailability of this peptide, we have coupled to the N-terminus of conotoxin MII, 2-amino-D,L-dodecanoic acid (Laa) creating a lipidic linear peptide which was then successfully oxidised to produce the correctly folded conotoxin MII construct.

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Link to publisher version (DOI)

http://dx.doi.org/10.1023/A:1016577832311