tailieunhanh - Báo cáo khoa học: Interaction of the P-type cardiotoxin with phospholipid membranes

The cardiotoxin (cytotoxin II, or CTII) isolated from cobra snake (Naja oxiana) venom is a 60-residue basic membrane-activeprotein featuring three-fingerbetasheet 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 (Pam2 Gro-PCho) or dipalmitoylglycerophosphoglycerol (Pam2 Gro-PGro), res-pectively. . | Eur. J. Biochem. 270 2038-2046 2003 FEBS 2003 doi Interaction of the P-type cardiotoxin with phospholipid membranes Peter V. Dubovskii Dmitry M. Lesovoy Maxim A. Dubinnyi Yuri N. Utkin and Alexander S. Arseniev Shemyakin Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russian Federation The cardiotoxin cytotoxin II or CTII isolated from cobra snake Naja oxiana venom is a 60-residue basic membraneactive protein featuring three-finger beta sheet fold. To assess possible modes of CTII membrane interaction 31P- and 1H-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 Pam2Gro-PCho or dipalmitoylglycerophosphoglycerol Pam2Gro-PGro respectively. The analysis of H-NMR linewidths of the toxin and 31P-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 Pam2Gro-PCho membranes was not observed b penetrating mode hydrophobic interactions develop due to penetration of the toxin into Pam2Gro-PGro 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 toxinmembrane interactions .

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