Publication: Evaluation of the binding mechanism of human defensin 5 in a bacterial membrane: A simulation study
Issued Date
2021-11-01
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ISSN
14220067
16616596
16616596
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2-s2.0-85119103526
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Mahidol University
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SCOPUS
Bibliographic Citation
International Journal of Molecular Sciences. Vol.22, No.22 (2021)
Suggested Citation
Tadsanee Awang, Phoom Chairatana, Ranjit Vijayan, Prapasiri Pongprayoon Evaluation of the binding mechanism of human defensin 5 in a bacterial membrane: A simulation study. International Journal of Molecular Sciences. Vol.22, No.22 (2021). doi:10.3390/ijms222212401 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/75971
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Title
Evaluation of the binding mechanism of human defensin 5 in a bacterial membrane: A simulation study
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Abstract
Human α-defensin 5 (HD5) is a host-defense peptide exhibiting broad-spectrum antimicrobial activity. The lipopolysaccharide (LPS) layer on the Gram-negative bacterial membrane acts as a barrier to HD5 insertion. Therefore, the pore formation and binding mechanism remain unclear. Here, the binding mechanisms at five positions along the bacterial membrane axis were investigated using Molecular Dynamics. (MD) simulations. We found that HD5 initially placed at positions 1 to 3 moved up to the surface, while HD5 positioned at 4 and 5 remained within the membrane interacting with the middle and inner leaflet of the membrane, respectively. The arginines were key components for tighter binding with 3-deoxy-d-manno-octulosonic acid (KDO), phosphates of the outer and inner leaflets. KDO appeared to retard the HD5 penetration.