Format

Send to:

Choose Destination
See comment in PubMed Commons below
Mar Drugs. 2014 Jun 5;12(6):3449-65. doi: 10.3390/md12063449.

Characterization of a novel Conus bandanus conopeptide belonging to the M-superfamily containing bromotryptophan.

Author information

  • 1Neurobiology and Development Laboratory, Research Unit # 3294, Institute of Neurobiology Alfred Fessard # 2118, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France. nguyenbaocbp@yahoo.com.
  • 2Research Unit # 2301, Natural Product Chemistry Institute, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France. jean-pierre.lecaer@icsn.cnrs-gif.fr.
  • 3Molecular Engineering of Proteins, Institute of Biology and Technology Saclay, Atomic Energy Commission, Gif sur Yvette Cedex 91191, France. gilles.mourier@cea.fr.
  • 4Molecular Engineering of Proteins, Institute of Biology and Technology Saclay, Atomic Energy Commission, Gif sur Yvette Cedex 91191, France. robert.thai@cea.fr.
  • 5Neurobiology and Development Laboratory, Research Unit # 3294, Institute of Neurobiology Alfred Fessard # 2118, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France. lamthanh5hung@yahoo.fr.
  • 6Molecular Engineering of Proteins, Institute of Biology and Technology Saclay, Atomic Energy Commission, Gif sur Yvette Cedex 91191, France. denis.servent@cea.fr.
  • 7Neurobiology and Development Laboratory, Research Unit # 3294, Institute of Neurobiology Alfred Fessard # 2118, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France. Evelyne.Benoit@inaf.cnrs-gif.fr.
  • 8Neurobiology and Development Laboratory, Research Unit # 3294, Institute of Neurobiology Alfred Fessard # 2118, National Center for Scientific Research, Gif sur Yvette Cedex 91198, France. jordi.molgo@inaf.cnrs-gif.fr.

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.

PMID:
24905483
[PubMed - indexed for MEDLINE]
PMCID:
PMC4071585
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Multidisciplinary Digital Publishing Institute (MDPI) Icon for PubMed Central
    Loading ...
    Write to the Help Desk