Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR.

作者: Koh Takeuchi , Hideo Takahashi , Mariko Sugai , Hideo Iwai , Toshiyuki Kohno

DOI: 10.1074/JBC.M307815200

关键词: MoleculeProtein structureSurface plasmon resonanceLiposomeBiophysicsPhospholipidCrystallographyMembraneVesicleChemistryPeptide sequence

摘要: The action mechanism of sapecin, an antibacterial peptide with membrane permeabilization activity, was investigated. dose dependence the caused by sapecin sigmoidal, suggesting that oligomerization leads to permeabilization. Solution nuclear magnetic resonance analysis sapecin-phospholipid vesicle complex revealed surface buried in and on molecule. membrane-buried determined observing transferred cross-saturation phenomena from alkyl chains phospholipid amide protons sapecin. contains basic highly exposed hydrophobic residues, which are suitable for interacting acidic bacterial membrane. also identified comparisons between results hydrogen-deuterium exchange experiments experiments. On basis NMR we built a putative model oligomers, provides insights into insect defensins.

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