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- W2912100491 abstract "Defensins are cationic cysteine-rich small molecules with molecular masses ranging from 3 to 5 kDa. Human β defensin (hBD) type 3 (hBD-3) is mainly secreted from epithelial cells, and it is important to the human innate immune system. It has broad-spectrum of antimicrobial activities on virus, fungi, and both Gram-positive and Gram-negative bacteria. hBD-3 has a charge density of +11. It can selectively interact with negatively charged bacteria lipid membrane without disrupting the mammalian cell membrane at the same concentration attacking bacterial lipid membrane. In this project, the interaction and binding of hBD-3 with different kinds of negatively charged lipid bilayers was investigated using molecular dynamics simulations. In total, three kinds of lipid bilayers: POPS, POPG, POPC+10%PIP2 were set up. In order to consider the hBD-3 structure effect on the binding, besides hBD-3 wildtype, hBD-3 analog which has three disulfide bonds removed, was also studied. Since hBD-3 can form a dimer, the binding of hBD-3 in both monomer and dimer forms with lipid membranes were investigated as well. The structure of hBD-3 on lipid membranes and the key residues on the binding interface between hBD-3 and lipid membranes were explored and compared. hBD-3 analog shows more interaction with the lipid membrane than the wildtype, and it has a more compacted structure around lipid membranes than in solvent. Moreover, in different lipid bilayers, the dynamics and the complex structures of hBD-3 and lipid membranes are different. Thus, it is expected that lipid head groups can influence the antibacterial function of hBD-3." @default.
- W2912100491 created "2019-02-21" @default.
- W2912100491 creator A5081478540 @default.
- W2912100491 date "2019-02-01" @default.
- W2912100491 modified "2023-09-30" @default.
- W2912100491 title "Binding of Human Beta Defensin Type 3 with Negatively Charged Lipid Membranes" @default.
- W2912100491 doi "https://doi.org/10.1016/j.bpj.2018.11.2747" @default.
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