Journal
MARINE DRUGS
Volume 12, Issue 6, Pages 3449-3465Publisher
MDPI AG
DOI: 10.3390/md12063449
Keywords
Conus bandanus; cone snail venom; mass spectrometry; BnIIID; bromotryptophan; gamma-carboxy glutamate; post-translational modifications
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Funding
- French government (Embassy of France in Vietnam)
- National Center for Scientific Research
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A novel conotoxin (conopeptide) was biochemically characterized from the crude venom of the molluscivorous marine snail, Conus bandanus (Hwass in Bruguiere, 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, gamma-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 (-CCx(1)x(2)x(3)x(4)Cx(1)x(2)x(3)Cx(1)CC-) 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.
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