NR study into the selective binding of designed short amphiphilic antimicrobial peptides into model lipid membranes
Bacterial infections are becoming increasingly complicated to treat due to the ability of bacteria to gain resistance against many of currently used antibiotics. Antimicrobial peptides have been widely studied as potential antibacterial drugs to combat antimicrobial resistance. In our previous studies we have examined a series of designed amphiphilic AMPs with the sequence of G(IIKK)n-I-NH2 where n denotes the number of α-helical repeats (n=2-4, denoted as G2, G3 and G4). The G3 and G4 peptides have been shown to possess strong but also different antibacterial activity against both gram-positive and gram-negative bacteria. These designed peptides were structurally optimised, so they show better efficacy and better biocompatibility than most AMPs reported, natural or designed. However, we still do not have the molecular level of understanding about the exact mechanistic processes that lead to the effective killing of bacteria cells and mildness to mammalian host cells. Neutron reflection (NR) work as described here aims to provide more direct insight regarding the membrane disruption mechanism of G4 using model lipid monolayers mimicking the membrane of gram-negative bacteria.
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Jian Ren Lu; Richard A. Campbell; CIUMAC Daniela; FA Ke and GONG Haoning. (2018). NR study into the selective binding of designed short amphiphilic antimicrobial peptides into model lipid membranes. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-730
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