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

Katsumi Matsuzaki, Shuji Yoneyama, Nobutaka Fujii, Koichiro Miyajima, Ken Ichi Yamada, Yutaka Kirino, Kazunori Anzai

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119 Citations (Scopus)


Tachyplesin I (T-SS), an antimicrobial peptide from Tachypleus tridentatus, has a cyclic antiparallel β-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., and 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.

Original languageEnglish
Pages (from-to)9799-9806
Number of pages8
Issue number32
Publication statusPublished - Aug 12 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry


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