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- W2020328077 abstract "The cardiotoxin (cytotoxin II, or CTII) isolated from cobra snake ( Naja oxiana ) venom is a 60‐residue basic membrane‐active protein featuring three‐finger beta sheet fold. To assess possible modes of CTII/membrane interaction 31 P‐ and 1 H‐NMR spectroscopy was used to study binding of the toxin and its effect onto multilamellar vesicles (MLV) composed of either zwitterionic or anionic phospholipid, dipalmitoylglycerophosphocholine (Pam 2 Gro‐ P Cho) or dipalmitoylglycerophosphoglycerol (Pam 2 Gro‐ P Gro), respectively. The analysis of 1 H‐NMR linewidths of the toxin and 31 P‐NMR spectral lineshapes of the phospholipid as a function of temperature, lipid‐to‐protein ratios, and pH values showed that at least three distinct modes of CTII interaction with membranes exist: (a) nonpenetrating mode; in the gel state of the negatively charged MLV the toxin is bound to the surface electrostatically; the binding to Pam 2 Gro‐ P Cho membranes was not observed; (b) penetrating mode; hydrophobic interactions develop due to penetration of the toxin into Pam 2 Gro‐ P Gro membranes in the liquid‐crystalline state; it is presumed that in this mode CTII is located at the membrane/water interface deepening the side‐chains of hydrophobic residues at the tips of the loops 1–3 down to the boundary between the glycerol and acyl regions of the bilayer; (c) the penetrating mode gives way to isotropic phase, stoichiometrically well‐defined CTII/phospholipid complexes at CTII/lipid ratio exceeding a threshold value which was found to depend at physiological pH values upon ionization of the imidazole ring of His31. Biological implications of the observed modes of the toxin–membrane interactions are discussed." @default.
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- W2020328077 date "2003-04-11" @default.
- W2020328077 modified "2023-10-18" @default.
- W2020328077 title "Interaction of the P-type cardiotoxin with phospholipid membranes" @default.
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- W2020328077 doi "https://doi.org/10.1046/j.1432-1033.2003.03580.x" @default.
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