Kinetics of cryptdin-4 translocation coupled with peptide-induced vesicle leakage
Kinetics of cryptdin-4 translocation coupled with peptide-induced vesicle leakage
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DOI：
10.1021/bi701110m
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发表时间：
2007-10-23
期刊：
影响因子：
2.9
通讯作者：
Vanderlick, T. Kyle
中科院分区：
文献类型：
--
作者：
Cummings, Jason E.;Vanderlick, T. Kyle
抗微生物肽Cryptdin-4（Crp 4）是α-防御素家族的成员，其显示出协同地跨磷脂双层易位。该过程的协同性通过随肽与脂质的摩尔比而变化的移位动力学来表现。一个简单的缔合模型表明二聚化。黑色脂质膜实验表明，Crp 4易位不会产生明确的水孔，这在表现出协同易位的肽中通常是常见的。尽管如此，由Crp 4诱导的流出后，其与荧光团加载囊泡的相互作用被证明是一个直接的结果，从易位过程中产生的膜扰动。渗漏可以通过将膜渗透性与移位的肽的分数相关联来预测。Crp 4易位对其抗微生物活性有影响，因为内化的肽可用于攻击细胞内靶标。
The antimicrobial peptide cryptdin-4 (Crp4), a member of the alpha-defensin family, is shown to translocate cooperatively across phospholipid bilayers. The cooperativity of the process is manifested by translocation kinetics which vary with the peptide to lipid molar ratio. A simple association model suggests dimerization. Black lipid membrane experiments reveal that Crp4 translocation does not create well-defined aqueous pores, as is often common among peptides exhibiting cooperative translocation. Still, the efflux induced by Crp4 upon its interaction with fluorophore-loaded vesicles is shown to be a direct result of the membrane perturbation resulting from the translocation process. Leakage can be predicted by relating membrane permeability to the fraction of peptide translocated. Crp4 translocation has implications for its antimicrobial activity as internalized peptide would be available to attack intracellular targets.