Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.
Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.
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DOI：
10.1021/bi900914g
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发表时间：
2009-09-01
期刊：
影响因子：
2.9
通讯作者：
Pokorny A
中科院分区：
文献类型：
--
作者：
Almeida PF;Pokorny A
六种不同的抗菌，溶细胞和细胞穿透肽，包括它们的一些变体的机制进行了讨论和比较。这些多肽的特异性各不相同，但它们在与膜结合时都形成两亲性α-螺旋，并且它们的序列没有显著差异。我们研究了它们与磷脂囊泡相互作用的热力学和动力学，即结合和肽诱导的染料流出。结合的热力学计算使用Wimley-White界面疏水性尺度与实验得出的值吻合得很好。结合亲和力决定功能特异性的普遍接受的观点也得到了模型膜实验的支持。我们现在提出的假设，这是热力学的肽插入到膜，从表面结合状态，这决定了机制。
The mechanisms of six different antimicrobial, cytolytic, and cell-penetrating peptides, including some of their variants, are discussed and compared. The specificity of these polypeptides varies, but they all form amphipathic α-helices when bound to membranes, and there are no striking differences in their sequences. We have examined the thermodynamics and kinetics of their interaction with phospholipid vesicles, namely binding and peptide-induced dye efflux. The thermodynamics of binding calculated using the Wimley-White interfacial hydrophobicity scale are in good agreement with the values derived from experiment. The generally accepted view that binding affinity determines functional specificity is also supported by experiment in model membranes. We now propose the hypothesis that it is the thermodynamics of peptide insertion into the membrane, from a surface-bound state, that determines the mechanism.
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影响因子：
4.8
作者：
Derossi, D;Calvet, S;Prochiantz, A
通讯作者：
Prochiantz, A
影响因子：
3.4
作者：
Hällbrink, M;Florén, A;Langel, Ü
通讯作者：
Langel, Ü
影响因子：
3.5
作者：
BESSALLE, R;KAPITKOVSKY, A;FRIDKIN, M
通讯作者：
FRIDKIN, M
影响因子：
8
作者：
BECHINGER, B;ZASLOFF, M;OPELLA, SJ
通讯作者：
OPELLA, SJ
影响因子：
--
作者：
BENNAIM, A
通讯作者：
BENNAIM, A