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Mar. Drugs 2014, 12(6), 3449-3465; doi:10.3390/md12063449
Article

Characterization of a Novel Conus bandanus Conopeptide Belonging to the M-Superfamily Containing Bromotryptophan

1,2
, 3
, 4
, 4
, 1,2
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 and 1,*
1 Neurobiology and Development Laboratory, Research Unit # 3294, Institute of Neurobiology Alfred Fessard # 2118, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France 2 Institute of Biotechnology and Environment, University of Nha Trang, Nha Trang, Khanh Hoa 57000, Vietnam 3 Research Unit # 2301, Natural Product Chemistry Institute, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France 4 Molecular Engineering of Proteins, Institute of Biology and Technology Saclay, Atomic Energy Commission, Gif sur Yvette Cedex 91191, France
* Author to whom correspondence should be addressed.
Received: 21 February 2014 / Revised: 7 March 2014 / Accepted: 22 May 2014 / Published: 5 June 2014
(This article belongs to the Special Issue Advances and New Perspectives in Marine Biotechnology)
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Abstract

A novel conotoxin (conopeptide) was biochemically characterized from the crude venom of the molluscivorous marine snail, Conus bandanus (Hwass in Bruguière, 1792), collected in the south-central coast of Vietnam. The peptide was identified by screening bromotryptophan from chromatographic fractions of the crude venom. Tandem mass spectrometry techniques were used to detect and localize different post-translational modifications (PTMs) present in the BnIIID conopeptide. The sequence was confirmed by Edman’s degradation and mass spectrometry revealing that the purified BnIIID conopeptide had 15 amino acid residues, with six cysteines at positions 1, 2, 7, 11, 13, and 14, and three PTMs: bromotryptophan, γ-carboxy glutamate, and amidated aspartic acid, at positions “4”, “5”, and “15”, respectively. The BnIIID peptide was synthesized for comparison with the native peptide. Homology comparison with conopeptides having the III-cysteine framework (–CCx1x2x3x4Cx1x2x3Cx1CC–) revealed that BnIIID belongs to the M-1 family of conotoxins. This is the first report of a member of the M-superfamily containing bromotryptophan as PTM.
Keywords: Conus bandanus; cone snail venom; mass spectrometry; BnIIID; bromotryptophan; γ-carboxy glutamate; post-translational modifications Conus bandanus; cone snail venom; mass spectrometry; BnIIID; bromotryptophan; γ-carboxy glutamate; post-translational modifications
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Nguyen, B.; Caer, J.-P.L.; Mourier, G.; Thai, R.; Lamthanh, H.; Servent, D.; Benoit, E.; Molgó, J. Characterization of a Novel Conus bandanus Conopeptide Belonging to the M-Superfamily Containing Bromotryptophan. Mar. Drugs 2014, 12, 3449-3465.

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