David, SA and Mathan, VI and Balaram, Padmanabhan (1992) Interaction of melittin with endotoxic lipid. In: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1123 (3). 269-274 .
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Several amphipathic and cationic substances are known to bind lipid A, the toxic component of bacterial lipopolysaccharides. In this report, we have characterized, by fluorescence methods, the interaction of melittin, an amphipathic and basic 26-residue polypeptide isolated from bee venom, with lipid A. The stoichiometry of the complex appears to be two molecules of melittin to one of lipid A with a dissociation constant of 2.5 × 10 −6 M. The binding of melittin not only modifies the endotoxic properties of lipid A in a number of biological assays, but also results in abrogation of the hemolytic activity of melittin. A model of the complex is proposed based on the known structures of lipid A and melittin, and the observed stoichiometry of binding.
|Item Type:||Journal Article|
|Additional Information:||copyright of this article belongs to Elsevier Science.|
|Keywords:||Melittin; Lipid A; Lipopolysaccharide; Fluorescence.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||11 Nov 2010 05:55|
|Last Modified:||11 Nov 2010 05:55|
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