چکیده

Antimicrobial peptides (AMPs) are short, cationic, membrane-interacting peptides that exhibit broad-spectrum antimicrobial activity. The peptides are a group within water/bilayer soluble peptide toxins used in all organisms defence and offense systems. AMPs are excellent candidates for development as novel therapeutic agents and complement conventional antibiotics therapy. Herein, we investigate the structure, dynamics, and membrane perturbing potency of three AMPs (Pardaxin, Pleurocidin, and GF-17) into the different bilayers using all-atom molecular dynamics (MD) simulation. The results revealed that paradaxin could markedly deform the structure of palmitoyl-oleoyl-phosphatidylcholine (POPC) lipid bilayers. In contrast, the peptide could not significantly affect the structure of palmitoyl-oleoyl-phosphatidylglycerol (POPG). The MD results indicated that pleurocidin interacted weakly with the neutral phospholipid bilayers (DOPC), making strong interactions with the negatively charged phospholipids. The results also showed that GF-17 is stabilized on the membrane surface and rapidly binds to the phosphate head groups of the model membranes through electrostatic interactions and hydrogen bonds. This research has provided data on the peptide-membrane interactions and the reasons for the resistance of the eukaryotic membrane to the peptides at atomic details that are useful for developing potent AMPs targeting multidrug-resistant bacteria.

کليدواژه ها

Molecular dynamics simulation, Antimicrobial peptides, Biomembranes

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فرامرز مهرنژاد , 1400 , مطالعه ساختار، دینامیک و عملکرد پپتیدهای ضد میکروبی در غشاهای زیستی با استفاده از شبیه سازی دینامیک مولکولی , نخستین همایش بین المللی و سومین همایش ملی ریاضیات زیستی