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Deciphering the mode of action of the synthetic antimicrobial peptide Bac8c.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Spindler, Eileen Colie Hale, John D. F. Giddings, Thomas H. Hancock, Robert E. W. Gill, Ryan T. |
| Copyright Year | 2011 |
| Abstract | Bac8c (RIWVIWRR-NH(2)) is an 8-amino-acid peptide derived from Bac2A (RLARIVVIRVAR-NH(2)), a C3A/C11A variant of the naturally occurring bovine peptide, bactenecin (also known as bovine dodecapeptide), the smallest peptide with activity against a range of pathogenic Gram-positive and Gram-negative bacteria, as well as yeast. The effects of Bac8c on Escherichia coli were examined by studying its bacteriostatic and bactericidal properties, demonstrating its effects on proton motive force generation, and visually analyzing (via transmission electron microscopy) its effects on cells at different concentrations, in order to probe the complexities of the mechanism of action of Bac8c. Results were consistent with a two-stage model for the Bac8c mode of action. At sublethal concentrations (3 μg/ml), Bac8c addition resulted in transient membrane destabilization and metabolic imbalances, which appeared to be linked to inhibition of respiratory function. Although sublethal concentrations resulted in deleterious downstream events, such as methylglyoxal formation and free radical generation, native E. coli defense systems were sufficient for full recovery within 2 h. In contrast, at the minimal bactericidal concentration (6 μg/ml), Bac8c substantially but incompletely depolarized the cytoplasmic membrane within 5 min and disrupted electron transport, which in turn resulted in partial membrane permeabilization and cell death. |
| Starting Page | 1596 |
| Ending Page | 1612 |
| Page Count | 17 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://aac.asm.org/content/55/4/1706.full.pdf |
| Alternate Webpage(s) | http://cmdr.ubc.ca/bobh/wp-content/uploads/2016/11/439.-Spindler-2011.pdf |
| PubMed reference number | 21282431v1 |
| Alternate Webpage(s) | https://doi.org/10.1128/AAC.01053-10 |
| DOI | 10.1128/aac.01053-10 |
| Journal | Antimicrobial agents and chemotherapy |
| Volume Number | 55 |
| Issue Number | 4 |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Antimicrobial Peptide Cattle Cell Death Electron Transport Free Radicals Gram-Negative Bacteria Metabolic Process, Cellular Nesiritide Plasma membrane Proton-Motive Force Protons Pyruvaldehyde Respiratory Insufficiency Thioctic Acid Tissue membrane Transmission Electron Microscopy bactenecin gram methylglyoxal biosynthetic process |
| Content Type | Text |
| Resource Type | Article |
