Effect of Alamethicin on the Structure of Lipid Bilayers

  • Alamethicin is a 20-amino acid membrane-active peptide from the fungus Trichoderma viride that spontaneously inserts into lipid membranes and self-associates into transmembrane channels. It has an antimicrobial activity against fungi and Gram-positive bacteria. We have investigated the effect of the peptide on the structure of lipid membranes by X-ray scattering method. The highly aligned stacks of membranes were prepared by evaporation of organic solutions of alamethicin and 1,2-dioleoyl-sn-glycero-3-phosphocholine deposited on clean silicon surfaces and were immersed in excess ultra pure water. The in-situ X-ray measurements show that the membranes with inserted peptides become thinner and softer at high molar peptide/lipid ratio.
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  • [1] . Zasloff M. Nature, 2002, 415(6870): 3892. Sansom M S P. Eur. Biophys. J., 1993, 22: 1053. Sansom M S P. Prog. Biophys. Molec. Biol., 1991, 55: 1394. Bechinger B. Biochim. Biophys. Acta, 1999, 1462: 1575. Shai Y. Biochim. Biophys. Acta, 1999, 1462: 556. de Grado W F, Musso G F et al. Biophys. J., 1982, 37: 3297. Tosteson M T, Holmes S J et al. J. Membrane Biol., 1985,87: 358. HUANG H, WU Y. Biophys. J., 1991, 60: 10799. Ludtke S, HE K, HUANG H. Biochemistry, 1995, 34:1676410. HE K, Ludtke S J et al. Biophys. J., 1996, 71: 266911. Kikukawa T, Araiso T. Arch. Biochem. Biophys., 2002,405: 21412. HUANG H W, CHEN F Y, Lee M T. Phys. Rev. Lett.,2004, 92: 19830413. LI C H, Constantin D, Salditt T. J. Phys.: Condens. Mat-ter, 2004, 16: S243914. Rand R P, Parsegian V A. Biochim. Biophys. Acta, 1989,988: 35115. HU S X, LI X H, JIA Q J et al. J. Chem. Phys., 2005, 122:12471216. JIANG X, ZHENG W, WU J et al. Rev. Sci. Instrum.,1995, 66(2): 169417. LI X H, LI M, MAI Z H. J. Phys. Chem., 2004, B108: 833818. Goulian M, Bruinsma R, Pincus P. Europhys. Lett., 1993,22: 14519. DAN N, Berman A et al. J. Phys. (Paris), 1994, 4: 171320. Fournier J B. Phys. Rev. Lett., 1996, 76: 443621. Weikl T R, Kozlov M M, Helfrich W. Phys. Rev., 1998,E57: 698822. CHEN C M. Physica, 2000, A281: 4123. Spaar A, Munster C, Salditt T. Biophys. J., 2004, 87: 396
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LI Da-Peng, HU Shu-Xin, MAI Zhen-Hong and LI Ming. Effect of Alamethicin on the Structure of Lipid Bilayers[J]. Chinese Physics C, 2005, 29(S1): 1-3.
LI Da-Peng, HU Shu-Xin, MAI Zhen-Hong and LI Ming. Effect of Alamethicin on the Structure of Lipid Bilayers[J]. Chinese Physics C, 2005, 29(S1): 1-3. shu
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Received: 2005-10-13
Revised: 1900-01-01
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Effect of Alamethicin on the Structure of Lipid Bilayers

    Corresponding author: LI Ming,
  • Institute of Physics,Chinese Academy of Sciences,Beijing 100080,China

Abstract: Alamethicin is a 20-amino acid membrane-active peptide from the fungus Trichoderma viride that spontaneously inserts into lipid membranes and self-associates into transmembrane channels. It has an antimicrobial activity against fungi and Gram-positive bacteria. We have investigated the effect of the peptide on the structure of lipid membranes by X-ray scattering method. The highly aligned stacks of membranes were prepared by evaporation of organic solutions of alamethicin and 1,2-dioleoyl-sn-glycero-3-phosphocholine deposited on clean silicon surfaces and were immersed in excess ultra pure water. The in-situ X-ray measurements show that the membranes with inserted peptides become thinner and softer at high molar peptide/lipid ratio.

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