Title |
Single molecule resolution of the antimicrobial action of quantum dot-labeled sushi peptide on live bacteria
|
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Published in |
BMC Biology, May 2009
|
DOI | 10.1186/1741-7007-7-22 |
Pubmed ID | |
Authors |
Sebastian Leptihn, Jia Yi Har, Jianzhu Chen, Bow Ho, Thorsten Wohland, Jeak Ling Ding |
Abstract |
Antimicrobial peptides are found in all kingdoms of life. During the evolution of multicellular organisms, antimicrobial peptides were established as key elements of innate immunity. Most antimicrobial peptides are thought to work by disrupting the integrity of cell membranes, causing pathogen death. As antimicrobial peptides target the membrane structure, pathogens can only acquire resistance by a fundamental change in membrane composition. Hence, the evolution of pathogen resistance has been a slow process. Therefore antimicrobial peptides are valuable alternatives to classical antibiotics against which multiple drug-resistant bacteria have emerged. For potential therapeutic applications as antibiotics a thorough knowledge of their mechanism of action is essential. Despite the increasingly comprehensive understanding of the biochemical properties of these peptides, the actual mechanism by which antimicrobial peptides lyse microbes is controversial. |
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Other | 5 | 6% |
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Immunology and Microbiology | 6 | 8% |
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