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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Interaction of bee venom toxin melittin with ganglioside GM1 bicelle
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Interaction of bee venom toxin melittin with ganglioside GM1 bicelle

机译：Bee Venom Toxin Melittin与神经节GM1 Bicelle的相互作用

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摘要

Melittin is a bee venom toxin that can act as antimicrobial peptide. Gangliosides are glycosphingolipids that help maintain membrane structure and organization as well as act as anchors for lectins, toxins, pathogens and antimicrobial peptides. Here we investigate interaction of melittin with fast tumbling isotropic control DMPC/CHAPS bicelles and ganglioside doped DMPC/CHAPS/GM1 bicelles. DOSY result shows that larger percentage of peptide binds to GM1 containing bicelles than that of the control PC bicelles. Bound peptide induces leakage of the bicelles entrapped carboxyfluorescein. Percentage of leakage is higher from control PC bicelles than that of the GM1 containing bicelles. In the presence of control PC bicelles melittin acquired fully alpha-helical structure. But in the presence of GM1 containing bicelles the peptide is not fully alpha-helical i.e., some random coil structure is present in this folded form. The present study shows that GM1 has an effect on membrane active antimicrobial peptide melittin.
机译：Melittin是一种蜜蜂毒素，可以充当抗微生物肽。神经节苷脂是糖磷脂，可帮助维持膜结构和组织，并充当凝集素，毒素，病原体和抗微生物肽的锚。在这里，我们研究了Melittin的相互作用与快速翻滚的各向同性对照DMPC / CHAPS BICelles和Ganglioside掺杂DMPC / CHAPS / GM1 BICLES。 MoSY结果表明，较大百分比的肽与含有比对照PC散离的GM1结合。结合的肽诱导突出的羧基杂志素的泄漏。泄漏百分比从对照PC双裂隙率高于含有含有双裂的GM1的偏差。在控制PC的存在下，Bicelles Melittin获得了完全α-螺旋结构。但是在含有双椰子的GM1存在下，肽不是完全α-螺旋形的即，在这种折叠形式中存在一些随机线圈结构。本研究表明，GM1对膜活性抗微生物肽熔母有影响。

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