How do Self-Assembling Antimicrobial Lipopeptides Kill Bacteria?
| Autor: | John R. P. Webster, Frances Separovic, Jack Hart, Luke A. Clifton, Jessica Carter, Andrew J. McBain, Mingrui Liao, Hai Xu, Stephen M. King, Mario Campana, Marc-Antoine Sani, Ke Fa, Thomas A. Waigh, Peter Hollowell, Peixun Li, Haoning Gong, Shiying Zhu, Xuzhi Hu, Jian R. Lu, Armando Maestro |
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| Rok vydání: | 2020 |
| Předmět: |
Protein Conformation
alpha-Helical Staphylococcus aureus Circular dichroism Materials science Antimicrobial peptides Nanofibers Peptide Microbial Sensitivity Tests 02 engineering and technology 010402 general chemistry Hemolysis 01 natural sciences Hydrophobic effect Lipopeptides Anti-Infective Agents Escherichia coli Fluorescence microscope Humans Surface Tension General Materials Science Amino Acid Sequence Lipid bilayer chemistry.chemical_classification 021001 nanoscience & nanotechnology Antimicrobial 0104 chemical sciences Microscopy Fluorescence chemistry Drug Design Nanofiber Liposomes Biophysics 0210 nano-technology Antimicrobial Cationic Peptides |
| Zdroj: | Gong, H, Sani, M, Hu, X, Fa, K, Hart, J W, Liao, M, Hollowell, P, Carter, J, Clifton, L A, Campana, M, Li, P, King, S M, Webster, J R P, Maestro, A, Zhu, S, Separovic, F, Waigh, T A, Xu, H, Mcbain, A J & Lu, J R 2020, ' How do Self-Assembling Antimicrobial Lipopeptides Kill Bacteria? ', ACS applied materials & interfaces, vol. 12, no. 50, pp. 55675-55687 . https://doi.org/10.1021/acsami.0c17222 |
| ISSN: | 1944-8252 1944-8244 |
| Popis: | Antimicrobial peptides are promising alternatives to traditional antibiotics. A group of self-assembling lipopeptides was formed by attaching an acyl chain to the N-terminus of α-helix-forming peptides with the sequence Cx-G(IIKK)yI-NH2 (CxGy, x = 4–12 and y = 2). CxGy self-assemble into nanofibers above their critical aggregation concentrations (CACs). With increasing x, the CACs decrease and the hydrophobic interactions increase, promoting secondary structure transitions within the nanofibers. Antimicrobial activity, determined by the minimum inhibition concentration (MIC), also decreases with increasing x, but the MICs are significantly smaller than the CACs, suggesting effective bacterial membrane-disrupting power. Unlike conventional antibiotics, both C8G2 and C12G2 can kill Staphylococcus aureus and Escherichia coli after only minutes of exposure under the concentrations studied. C12G2 nanofibers have considerably faster killing dynamics and lower cytotoxicity than their nonaggregated monomers. Antimicrobial activity of peptide aggregates has, to date, been underexploited, and it is found to be a very promising mechanism for peptide design. Detailed evidence for the molecular mechanisms involved is provided, based on superresolution fluorescence microscopy, solid-state nuclear magnetic resonance, atomic force microscopy, neutron scattering/reflectivity, circular dichroism, and Brewster angle microscopy. |
| Databáze: | OpenAIRE |
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