Membrane pore formation by the lytic peptide KLA1: BENSC User Meeting 2004

D. Kim, Beate Maria Klösgen-Buchkremer, M. Dathe, S. Bezrukow, Th. Gutberlet, S. Dante, Th. Hauss, R. Krastev

Publikation: AndetAndet bidragForskning


Antimicrobial peptides (AMPs) constitute a broad class of compounds varying in amino acid composition (typically 9 to 100 residues), structural motif (α-helical, β-sheet), and target membranes (gram-negative and/or gram-positive bacteria, mammalian cells). AMPs are membrane-active compounds, often charged and amphiphilic.
The exact details of the mode of action of AMPs on target membranes are currently the subject of investigation. There are essentially three models of AMP destabilization of lipid membranes, namely the so-called “carpet” (membrane solubilization and destabilization) and the “barrel-stave” (transmembrane pore formation) models. The third one is another pore model, involving a transitory toroidal pore.
Here we present results obtained by application of several methods to collect details about the effect of the synthetic AMP KLA1 on lipid model bilayers in the form of small unilamellar vesicles (SUVs), planar supported and also free membranes as well as from membrane stacks and giant unilamellar vesicles (GUVs). Results are presented from Cryo-TEM, SANS, neutron reflectometry, conductivity measurements and micromechanical measurements by micropipette aspiration. They are in favour of the model of dynamically fluctuating toroidal pores. Future experiments shall explore the location of the peptide in the membrane by use of a deuterated peptide version.
UdgiverHMI Berlin
StatusUdgivet - 2004


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