BINDING AND ACTION OF CECROPIN AND CECROPIN ANALOGS - ANTIBACTERIAL PEPTIDES FROM INSECTS
BINDING AND ACTION OF CECROPIN AND CECROPIN ANALOGS - ANTIBACTERIAL PEPTIDES FROM INSECTS
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DOI：
10.1016/0005-2736(88)90069-7
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发表时间：
1988-04-07
期刊：
影响因子：
--
通讯作者：
MERRIFIELD, RB
中科院分区：
文献类型：
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作者：
STEINER, H;ANDREU, D;MERRIFIELD, RB
以天蚕素脂质体为模型系统，研究了天蚕素的作用机制。如果脂质体净电荷为零或负，则双分子层被有效地破坏。具有受损N-末端螺旋的天蚕素类似物具有降低的膜破坏能力，这与其较低的抗菌活性相关。类似物的杀菌活性降低是由于与细菌的结合减少。抗菌肽杀死细菌的化学计量表明，足以形成单层的抗菌肽的量强烈地修饰细菌膜。虽然一些细菌对天蚕素有抗性，但它们确实以非生产性的方式结合了大量天蚕素。相反，哺乳动物红细胞通过避免天蚕素的结合来实现抗性。
The mechanism of action of cecropin was studied by using liposomes as a model system. The bilayer was efficiently destroyed if the liposome net charge was zero or negative. Cecropin analogues with an impaired N-terminal helix had reduced membraned disrupting abilities that correlate with their lower antibacterial activity. The reduced bactericidal activity of the analogues was rationalized in terms of reduced binding to bacteria. The stoichiometry of cecropin killing of bacteria suggests that amounts of cecropin sufficient to form a monolayer strongly modify the bacterial membrane. Although some bacteria were resistant to cecropin they did bind large amounts in a non-productive manner. In contrast, mammalian erythrocytes achieve resistance by avoiding the binding of cecropin.