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Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog

机译：环状抗菌肽速激肽I及其线性类似物的膜通透性机制

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摘要

Tachyplesin I (T-SS), an antimicrobial peptide from Tachypleus tridentatus, has a cyclic antiparallel beta-sheet structure maintained by two disulfide bridges. The peptide effectively permeabilizes both bacterial and artificial lipid membranes. T-Acm, a linear analog peptide with the four SH groups protected by acetamidomethyl groups, exhibits a much weaker membrane-permeabilizing activity in spite of a greater disruption of the lipid organization [Matsuzaki, K., Nakayama, M., Fukui, M., Otaka, A., Funakoshi, S., Fujii, N., Bessho, K., & Miyajima, K. (1993) Biochemistry 32, 11704-11710]. To clarify the efficient permeabilization mechanism of T-SS, we studied the interactions of both peptides with liposomes and planar lipid bilayers. The cyclic peptide capable of spanning the bilayer (ca. 3 nm length) was found to form an anion-selective pore and translocate across the bilayer coupled with the pore formation. A cis-negative transmembrane potential facilitated the pore formation compared with the cis-positive potential. In contrast, the linear peptide failed to translocate. Instead, it impaired the membrane barrier by disrupting the lipid organization with morphological changes in the vesicles.
机译：Tachyplesin I（T-SS），一种来自Tachypleus tridentatus的抗菌肽，具有由两个二硫键维持的环状反平行β-折叠结构。该肽可有效渗透细菌膜和人工脂质膜。 T-Acm是带有乙酰氨基甲基保护的四个SH基团的线性类似物肽，尽管脂质组织的破坏更大，但其膜通透性却很弱[Matsuzaki，K.，Nakayama，M.，Fukui，M ，Otaka，A.，Funakoshi，S.，Fujii，N.，Bessho，K。和Miyajima，K。（1993）Biochemistry 32，11704-11710]。为了阐明T-SS的有效通透机制，我们研究了两种肽与脂质体和平面脂质双层的相互作用。发现能够跨越双层（约3nm长）的环状肽形成阴离子选择性孔，并跨过双层移位并与孔形成偶联。与顺式阳性电位相比，顺式阴性跨膜电位促进了孔的形成。相反，线性肽不能移位。相反，它通过破坏囊泡中形态变化的脂质组织来破坏膜屏障。

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