SANS study of the interaction between antimicrobial peptides and model phospholipid liposomes
We have previously demonstrated that designed cationic AMPs with the general sequence of G(IIKK)nI-NH2 (n=3,4) show great selective antibacterial ability in co-culturing experiments. The high selectivity is thought to be related to the difference in charges between different cell membranes. We have developed lipid vesicle models mimicking mammalian and bacterial (G-, G+) outer cell membranes by controlling charges, saturation and membrane composition. In our previous lab work including zeta potential measurements, liposomes’ size variation, Cryo-TEM and encapsulation of (6)-carboxyfluorescein (CF) leakage, we found that the liposome systems undergo charge reversal, leakage, damage or fusion upon interacting with our peptide G4. Small angle neutron scattering (SANS) is a powerful and unique technique to determine the variations of vesicular lipid bilayer structure and composition associated with these phenomena upon G4 peptide binding. Furthermore, it is possible to determine the peptide location by a combination of several isotopic contrasts involving deuterated lipids and different H2O:D2O ratios.
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Jian Ren Lu; CIUMAC Daniela; GRILLO Isabelle; KLUZEK Monika and LI Zongyi. (2016). SANS study of the interaction between antimicrobial peptides and model phospholipid liposomes. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-659
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