Role of modified glutamic acid in the helical structure of conantokin-T

FEBS Letters
C H LinP C Lyu

Abstract

Circular dichroism (CD) and 2-dimensional NMR were used to study the solution conformation of conantokin-T (Con-T), a small peptide toxin found in the venom of fish-hunting cone snails, and its Glu-substituted analog. Con-T lacks disulfide bonds but contains many gamma-carboxyglutamic acids (Gla), a post-translationally modified residue. Our results show that Con-T adopts an alpha-helical conformation in aqueous solution even in the absence of calcium. Glu replacements diminish both helicity and function of Con-T. The helical content of Con-T is higher than most natural helical peptides of this length in aqueous solution. The sequence of this small toxin incorporates several known elements that stabilize alpha-helical structure in peptides. Gla residues form several salt bridges that stabilize helical conformation of Con-T.

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Citations

Mar 31, 2004·Toxicon : Official Journal of the International Society on Toxinology·Estuardo López-VeraManuel B Aguilar
Feb 11, 2014·Toxicon : Official Journal of the International Society on Toxinology·Randall J PlattBaldomero M Olivera
Jul 16, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·T BlandlF J Castellino
Oct 6, 2009·Chemico-biological Interactions·Jon-Paul BinghamZachary L Bergeron
Aug 6, 1999·Protein Engineering·C H LinP C Lyu
Jan 13, 2004·Physiological Reviews·Heinrich Terlau, Baldomero M Olivera
Jul 21, 2006·The Journal of Physical Chemistry. B·Chung-Cheng WeiYing-Chieh Sun

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