Cardiotoxin, interactions with

Defourcq, ., Faucon,J.F., Bemard,E., Pezolot,M., Tessier,M., Bougis,R, Rietschoten, ., Delori,R, and Rochat,H., 1982, Structure-function relationships for the cardiotoxins interacting with phospholipids,... 

Various types of proteins have been purified using hydrophobic interaction chromatography including alkaline phophatase, estrogen receptors, isolectins, strepavidin, calmodulin, epoxide hydrolase, proteoglycans, hemoglobins, and snake venom toxins (46). In the case of cobra venom toxins, the order of elution of the six cardiotoxins supports the hypothesis that the mechanism of action is related to hydrophobic interactions with the phospholipids in the membrane. 

The effect of toxins such as melittin (from the honey-bee venom), myotoxin a, and cardiotoxin (from the snake venom) was investigated by vibrational spectroscopy (Pezolet et al., 1982 Faucon et ah, 1983 Liddle and Tu, 1985 Lafleur et ah, 1987). Monitoring the Raman intensity ratio I(1060)/I(1080) indicated that the lipid/melittin assemblies in DPPC are characterized by a high conformational order, little intermolecular chain-chain interaction, and a low cooperativity of the gel-like liquid crystalline phase transition. The effect of ricin, a toxic lectin, on DPPC and DPPC-cerebroside mixtures was studied by Raman and IR spectroscopy. It was suggested that ricin mainly interacts with the interfacial domains of the bilayers (Picquart et ah, 1989). 

Fasciculins belong to the structural family of threefingered toxins from Elapidae snake venoms, which include the a-neurotoxins that block the nAChR and the cardiotoxins that interact with cell membranes. The features unique to the known primary and tertiary structures of the fasciculin molecule were analyzed by Flarald et al. (1995). Loop I contains an arginine at position 11, which is found only in the fasciculins and could form a pivotal anchoring point to AChE. Loop II contains five cationic residues near its tip, which are partly charge-compensated by anionic side chains in loop III. 

Chien, K.Y, Chiang, C.M., Hseu, Y.U., Vyas, A.A., Rule, G.S., and Wu, W.G., 1994, Two distinct types of cardiotoxin as revealed by the stmcture and activity relationship of their interaction with zwitterionic phspholipid dispersions, J. Biol Chem. 269 14473-14483. 

Bougis, P, Tessier, M., Van Rietschoten, J., Rochat, H., Faucon, J.F. and Dufourcq, J., 1983, Are interactions with phospholipids responsible for pharmacological activities of cardiotoxins . Mol. Cell Biochem., 55 49. 

Dodecyl phosphocholine micelles in solution are useful and well characterized as a model membrane system for solution NMR studies. To access the membrane-induced conformation and orientation of cardiotoxins, the interaction of the p-type cardiotoxin II from Naja oxiana snake venom with perdeuterated dodecyl phosphocholine was studied by H NMR spectroscopy and diffusion measurements.247 2D NMR is an efficient tool and has been widely used to study the interaction of dodecyl phosphocholine with peptides and protein.248-250 2D... 

This study deals with the formation of complexes between blood clotting proteins and natural and artificial surfaces. As these surfaces are generally charged, the behavior of a basic protein, cardiotoxin (CTX), the interaction of which is strictly charge-dependent, is also reported for comparison. Two types of interface have been investigated. 

Cardiotoxin-polymer complexes. Finally, the interaction of CTX was also studied with a polymeric surface, PSSO2GIU, the composition and properties of which resemble those of heparin. As shown in Fig. 1, a result quite different from those for heparin or lipid binding is observed. When the surface is maximally covered, at a polymer to protein ratio of 12 mg of polymer per pmole of CTX, the quantum yield of Trp11 is decreased by about 50 %, while the emission wavelength remains almost unchanged at about 345 nm. This can be interpreted... 

Desormeaux, A., Laroche, G., Bougis, RE., and Pezolot, M., 1992, Characterisation by infrared spectroscopy of the interaction of a cardiotoxin with phosphatidic acid and with binary mixtures of phosphatidic acid and phosphatidyl choline. Biochemistry 31 12173-12182. 

Ksenzhek, O.S., Gerod, V.S., Omel Chenko, A.M., Semenov, S.N., Sotnichenkov, A.I., and Miro-schinikov, A.I., 1978, Interaction of the cardiotoxin of the venom of the cobra Naja naja oxiana with phospholipid membrane model system, A/b/. Biol. 12 1057-1065. 

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