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Determining the Structure and Orientation of the Alamethicin Ion Channel in Lipid Membranes using ATR and Electrochemical PMIRRAS

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Title: Determining the Structure and Orientation of the Alamethicin Ion Channel in Lipid Membranes using ATR and Electrochemical PMIRRAS
Author: Shodiev, Muzaffar
Department: Department of Chemistry
Program: Chemistry
Advisor: Lipkowski, Jacek
Abstract: Alamethicin is a short antibiotic peptide produced by the fungus Trichoderma viride. Ion channels formed by Alamethicin are voltage-gated due to their large molecular dipoles. The goals of this project were to monitor the incorporation of Alamethicin into 1,2-diphytanoyl-sn-glycero-3-phosphocholine (DPhPC) model biomimetic membranes and characterize the opening and closing of these incorporated Alamethicin channels. Attenuated Total Reflection Fourier Transform Infrared spectroscopy (ATR-FTIR) was employed to elucidate the mechanism of Alamethicin incorporation by first spreading vesicles onto the ATR prism. The IR signature of Alamethicin was determined and different peptide ratios were tested. In order to determine the opening and closing of the Alamethicin pore, a bilayer containing Alamethicin was deposited onto the surface of a thioglucose modified Au(111) electrode. Polarization Modulation Infrared Reflection Absorption Spectroscopy (PMIRRAS) was used to examine changes in the structure and orientation of Alamethicin as a function of the applied potential.
URI: http://hdl.handle.net/10214/8800
Date: 2015-05
Rights: Attribution-NonCommercial-NoDerivs 2.5 Canada


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Attribution-NonCommercial-NoDerivs 2.5 Canada Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 2.5 Canada