Pc16a, the first characterized peptide from Conus pictus venom, shows a novel disulfide connectivity.

Abstract:

:A novel conotoxin, pc16a, was isolated from the venom of Conus pictus. This is the first peptide characterized from this South-African cone snail and it has only 11 amino acid residues, SCSCKRNFLCC*, with the rare cysteine framework XVI and a monoisotopic mass of 1257.6Da. Two peptides were synthesized with two possible conformations: globular (pc16a_1) and ribbon (pc16a_2). pc16a_1 co-eluted with the native peptide, which indicates a disulfide connectivity I-III, II-IV. The structure of pc16a_1 was determined by NMR. Both synthetic peptides were used to elucidate the biological activity. Bioassays were performed on crickets, ghost shrimps, larvae of the mealworm beetle and mice, but no effect was seen. Using two-electrode voltage clamp, a range of voltage-gated ion channels (Na(v) and K(v)) and nicotinic acetylcholine receptors were screened, but again no activity was found. Hence, the specific target of pc16a still remains to be discovered.

journal_name

Peptides

journal_title

Peptides

authors

Van Der Haegen A,Peigneur S,Dyubankova N,Möller C,Marí F,Diego-García E,Naudé R,Lescrinier E,Herdewijn P,Tytgat J

doi

10.1016/j.peptides.2011.10.026

subject

Has Abstract

pub_date

2012-03-01 00:00:00

pages

106-13

issue

1

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(11)00466-9

journal_volume

34

pub_type

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