Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin.
Mar Drugs
; 16(6)2018 Jun 07.
Article
en En
| MEDLINE
| ID: mdl-29880743
ABSTRACT
The Australian jellyfish Chironex fleckeri, belongs to a family of cubozoan jellyfish known for their potent venoms. CfTX-1 and -2 are two highly abundant toxins in the venom, but there is no structural data available for these proteins. Structural information on toxins is integral to the understanding of the mechanism of these toxins and the development of an effective treatment. Two regions of CfTX-1 have been predicted to have helical structures that are involved with the mechanism of action. Here we have synthesized peptides corresponding to these regions and analyzed their structures using NMR spectroscopy. The peptide corresponding to the predicted N-terminal amphiphilic helix appears unstructured in aqueous solution. This lack of structure concurs with structural disorder predicted for this region of the protein using the Protein DisOrder prediction System PrDOS. Conversely, a peptide corresponding to a predicted transmembrane region is very hydrophobic, insoluble in aqueous solution and predicted to be structured by PrDOS. In the presence of SDS-micelles both peptides have well-defined helical structures showing that a membrane mimicking environment stabilizes the structures of both peptides and supports the prediction of the transmembrane region in CfTX-1. This is the first study to experimentally analyze the structure of regions of a C. fleckeri protein.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Venenos de Cnidarios
/
Cubomedusas
Tipo de estudio:
Prognostic_studies
/
Risk_factors_studies
Límite:
Animals
País/Región como asunto:
Oceania
Idioma:
En
Revista:
Mar Drugs
Asunto de la revista:
BIOLOGIA
/
FARMACOLOGIA
Año:
2018
Tipo del documento:
Article
País de afiliación:
Australia