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Interactions of human β-defensin 28 with solid supports mimicking bacterial and mammalian cell membranes

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Abstract

Development of resistance to conventional antibiotics by several bacterial strains is on the rise. To address this issue, antimicrobial peptides (AMPs) have recently proposed as alternatives to conventional antibiotics. Beside their excellent antimicrobial performance, these new antibiotics have less susceptibility to bacterial resistance development, making them safe and effective alternatives. Thus, this work presents a quantitative study on the interactions of human β-defensin 28 (an antimicrobial peptide) with bacterial-like (POPG-terminated) and mammalian-like (POPC-terminated) bilayer membranes. The first leaflet of both membranes was created through the self-assembly of thiolipid (TL) on the gold surface of a surface plasmon resonance (SPR) sensor chip. The second membrane leaflet was created by the fusion of either 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1-rac-glycerol) (abbreviated as POPG) or 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (abbreviated as POPC) phospholipid on the TL layer. The binding kinetics of human β-defensin 28 (hBD28) onto POPG and POPC surfaces were investigated. The surface saturation (Γmax) and affinity (Ka) of hBD28 for the POPG surface were estimated to be 4.51 ± 0.12 mg m−2 and 0.12 ± 0.01 mL μg−1, respectively. However, Γmax and Ka of the peptide (i.e., hBD28) for POPC surface were much lower: 1.65 mg m−2 and 0.03 mL μg−1, respectively. These findings suggest that hBD28 is reasonably selective towards pathogen-like membranes (i.e., POPG). hBD28 was also found to form an acceptably stable coating (via adsorption) on hydrophobic (TL) and negatively charged hydrophilic (11-mercaptoundecanoic acid, abbreviated as MUA) surfaces. The surface concentrations of the peptide on the TL and MUA surfaces at saturation were estimated to be 3.82 ± 0.32 and 4.47 ± 0.25 mg m−2, while its affinities for those surfaces were estimated to be 0.14 ± 0.05 and 0.13 ± 0.03 mL μg−1, respectively.

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Funding

This work was supported by the Deanship of Research Oversight and Coordination (DROC) at King Fahd University of Petroleum and Minerals (KFUPM) in the terms of Research Grant #DF191022.

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Authors and Affiliations

  1. Department of Chemical Engineering, King Fahd University of Petroleum and Minerals, Dhahran, 31261, Saudi Arabia

    Sagheer A. Onaizi

  2. Interdisciplinary Research Center for Hydrogen and Energy Storage, King Fahd University of Petroleum and Minerals, Dhahran, 31261, Saudi Arabia

    Sagheer A. Onaizi

  3. Food, Chemical and Biotechnology Cluster, Singapore Institute of Technology, 10 Dover Drive, Singapore, 138683, Singapore

    Susanna S.J. Leong

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  1. Sagheer A. Onaizi
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Both authors contributed to the study conception and design. Material preparation, data collection, and analysis were performed by both authors. The first draft of the manuscript was written by both authors. Both authors read and approved the final manuscript.

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Correspondence to Sagheer A. Onaizi.

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Onaizi, S.A., Leong, S.S. Interactions of human β-defensin 28 with solid supports mimicking bacterial and mammalian cell membranes. emergent mater. 7, 263–273 (2024). https://doi.org/10.1007/s42247-023-00601-0

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