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    Biophysical investigation into the antibacterial action of modelin-5-NH2

    Year: 2019

    Journal: Soft Matter, Volume 15, 1-May, page 4215–4226

    Authors: Dennison, Sarah R.; Hauss, Thomas; Badiani, Kamal; Harris, Frederick; Phoenix, David A.

    Organizations: European UnionEuropean Union (EU) [283883]; Biochemical Society Eric Reid Fund for Methodology

    Modelin-5-CONH2 (M5-NH2) is a synthetic antimicrobial peptide, which was found to show potent activity against Bacillus subtilis (minimum lethal concentration = 8.47 mu M) and to bind strongly to membranes of the organism (K-d = 10.44 mu M). The peptide adopted high levels of amphiphilic alpha-helical structure in the presence of these membranes (>50%), which led to high levels of insertion (Delta pi >= 8.0 mN m(-1)). M5-NH2 showed high affinity for anionic lipid (K-d = 7.46 mu M) and zwitterionic lipid (K-d = 14.7 mu M), which drove insertion into membranes formed from these lipids (Delta pi = 11.5 and 3.5 mN m(-1), respectively). Neutron diffraction studies showed that M5-NH2 inserted into B. subtilis membranes with its N-terminal residue, L16, located 5.5 angstrom from the membrane centre, in the acyl chain region of these membranes, and promoted a reduction in membrane thickness of circa 1.8 angstrom or 5% of membrane width. Insertion into B. subtilis membranes by the peptide also promoted other effects associated with membrane thinning, including increases in membrane surface area (C-s(-1) decreases) and fluidity (Delta G(mix) > 0 to Delta G(mix) < 0). Membrane insertion and thinning by M5-NH2 induced high levels of lysis (>55%), and it is speculated that the antibacterial action of the peptide may involve the toroidal pore, carpet or tilted-type mechanism of membrane permeabilization.
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