Abstract
Polyamino acids have been incorporated into extruded liposomes and the proton permeability of the liposomal membrane measured by fluorescence spectroscopy. This procedure was designed to test the theoretical possibility (Furois-Corbin and Pullman, 1986;1987) that a bundle of hydrophobic a-helices could provide a low energy pathway through the lipid bilayer for ions. Liposomes with incorporated poly-Lalanine or poly-L-leucine were found to have proton permeability coefficients 5–7 times greater than control liposomes, an effect similar to that seen with alamethicin in the same peptide to lipid range. Two molecular weights of polyalanine were tested for their effect on proton permeability. It was found that long-chain polyalanine (MW 24,600) had an effect 2.7 times greater than short-chain polyalanine (MW 2000). Poly-Lhistidine did not increase proton permeability above control values. Potassium permeability was not markedly increased by any of the polyamino acids tested. An analytical thin layer chromatography measurement of lipid and a fluorescamine assay for amino acids showed that there are ~300 polyleucine, ~400 long-chain polyalanine, or ~7600 short-chain polyalanine molecules associated with each liposome. Of the associated polyamino acid, Fourier transform infrared spectroscopy indicated that a major fraction exists in an a-helical conformation. Thus, hydrophobic polyamino acids in liposomes may represent a minimal model for proton channels.
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© 1992 Springer Science+Business Media Dordrecht
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Oliver, A.E., Deamer, D.W. (1992). A Minimal Model of Ion Channels: Polyamino Acids in Liposomes. In: Pullman, A., Jortner, J., Pullman, B. (eds) Membrane Proteins: Structures, Interactions and Models. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 25. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2718-9_27
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DOI: https://doi.org/10.1007/978-94-011-2718-9_27
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