Effect of Surface-Immobilized States of Antimicrobial Peptides on Their Ability to Disrupt Bacterial Cell Membrane Structure
Antimicrobial peptide (AMP) surfaces are widely used to inhibit biofilm formation and bacterial infection. However, endpoint-immobilized AMPs on surfaces are totally different from free-state AMPs due to the constraints of the surface. In this work, the interactions between AMPs and bacterial cell m...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-10-01
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| Series: | Journal of Functional Biomaterials |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-4983/15/11/315 |
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| Summary: | Antimicrobial peptide (AMP) surfaces are widely used to inhibit biofilm formation and bacterial infection. However, endpoint-immobilized AMPs on surfaces are totally different from free-state AMPs due to the constraints of the surface. In this work, the interactions between AMPs and bacterial cell membranes were analyzed through coarse-grained molecular dynamics and all-atom molecular dynamics simulations. This AMP disrupted membrane structure by altering the thickness and curvature of the membrane. Furthermore, the effect of surface-immobilized states of AMPs on their ability to disrupt membrane structure was revealed. The immobilized AMPs in the freeze-N system could bind to the membrane and disrupt the membrane structure through electrostatic forces between positively charged N-terminal amino acid residues and the negatively charged membrane, while the immobilized AMPs in the freeze-C system were repelled. The results will aid in the rational design of new AMP surfaces with enhanced efficacy and stability. |
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| ISSN: | 2079-4983 |