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  • Title: Alamethicin-lipid interaction studied by energy dispersive X-ray diffraction.
    Author: Domenici F, Panichelli D, Castellano AC.
    Journal: Colloids Surf B Biointerfaces; 2009 Mar 01; 69(2):216-20. PubMed ID: 19135341.
    Abstract:
    A detailed knowledge of the interaction between bacterial membranes and antibiotics provides important information to prevent high levels of antibiotic resistance exhibited by pathogenic strains. We investigated by energy dispersive X-ray diffraction (EDXD) the structure ordering of dioleoyl-phosphatidylcholine (DOPC) lipid interacting with antimicrobial peptide alamethicin, varying the lipid/peptide (L/P) molar ratio under two different hydration levels. In conditions of full hydration (100%) we found that the bilayer thickness is constant between L/P=20 and L/P=80 indicating that in this range, the system has reached the threshold value for the channel formation, while at the relative hydration of 45% a linear decrease of the bilayer thickness as function of L/P was revealed. The kinetic study of the complex alamethicin-DOPC at different L/P values, shows that the Bragg peak energy variation versus the hydration time has a biexponential behavior characterized by two different time constants.
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