作者: S.A. David , V.I. Mathan , P. Balaram
DOI: 10.1016/0005-2760(92)90006-H
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摘要: 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, interaction melittin, an basic 26-residue polypeptide isolated from bee venom, with A. The stoichiometry complex appears be two molecules melittin one A a dissociation constant 2.5 × 10 −6 M. binding not only modifies endotoxic properties in number biological assays, but also results abrogation hemolytic activity melittin. model is proposed based on structures observed binding.