Neutron reflection to study the interaction of designed -helix peptides with model lipid monolayers at the air/water interface
Increase of antibacterial resistance to antibiotics has led to huge international demand for developing new antibacterial agents with different mechanisms of action. Many natural antimicrobial peptides (AMPs) can disrupt bacterial membranes and kill them without causing resistance. Over the past 10 years or so, we have developed a series of rationally designed peptides with the general sequence G(IIKK)nI-NH2, with n-the number of coils of α-helix (n=2-4, denoted as G2, G3 and G4). These peptides are benign to mammalian cell hosts, exhibiting high mildness or biocompatibility. To help understand their membrane lytic actions and selective responses, we have developed lipid monolayer models using Langmuir film technique and characterized how our peptides interact with model G+, G- and red blood cell monolayer models consisting of 1, 2 and 3 membrane components. In the first part of our neutron reflection work, we aim to quantity how peptide G4 penetrated and associated with lipid monolayers focusing on the examination of charge and unsaturation. The known antimicrobial peptides will be used as controls, thus enabling us to make better comparison.
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Jian Ren Lu; Richard A. Campbell; CIUMAC Daniela; HOLMAN Robert and LI Zongyi. (2015). Neutron reflection to study the interaction of designed -helix peptides with model lipid monolayers at the air/water interface. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-611
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