The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
Open accessAbstract
Natural antimicrobial peptides (AMPs) provide prototypes for the design of unconventional antimicrobial agents. Existing bulk assays measure AMP activity but do not provide details of the growth-halting mechanism. We use fluorescence microscopy to directly observe the attack of the human antimicrobial peptide LL-37 on single Escherichia coli cells in real time. Our findings strongly suggest that disruption of the cytoplasmic membrane is not the growth-halting mechanism. At 8 μM, LL-37 binding saturates the outer membrane (OM) within 1 min. Translocation across the OM and access to the periplasmic space (5–25 min later) correlates in time with the halting of growth. Septating cells are attacked more readily than nonseptating cells. The halting of growth may occur because of LL-37 interference with cell wall biogenesis. Only well after growth halts does the peptide permeabilize the cytoplasmic membrane to GFP and the small dye Sytox Green. The assay enables dissection of antimicrobial design criteria into two parts: translocation across the OM and the subsequent halting of growth.
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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Determination of minimum inhibitory concentrations
Andrews, J. M. (2001) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/48.suppl_1.5 · Cited by 4,129
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Mookherjee, N., Anderson, M. A., Haagsman, H. P., & Davidson, D. J. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0058-8 · Cited by 1,502
The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms
de Breij, A., Riool, M., Cordfunke, R. A., Malanovic, N., de Boer, L., Koning, R. I., Ravensbergen, E., Franken, M., van der Heijde, T., Boekema, B. K., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan4044 · Cited by 555
The human cathelicidin LL-37 — A pore-forming antibacterial peptide and host-cell modulator
Xhindoli, D., Pacor, S., Benincasa, M., Scocchi, M., Gennaro, R., & Tossi, A. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.11.003 · Cited by 366
Antimicrobial Peptides: An Update on Classifications and Databases
Bin Hafeez, A., Jiang, X., Bergen, P. J., & Zhu, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111691 · Cited by 341
Analysis of Antimicrobial-Triggered Membrane Depolarization Using Voltage Sensitive Dyes
te Winkel, J. D., Gray, D. A., Seistrup, K. H., Hamoen, L. W., & Strahl, H. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00029 · Cited by 326
Metadata
- Authors
- Sochacki, K. A., Barns, K. J., Bucki, R., & Weisshaar, J. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-04-04
- Volume
- 108
- Issue
- 16
- Pages
- E77-81
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2046796256
- Cited by
- 267
- References
- 2
- FWCI
- 11.77
- Type
- journal article
- Language
- en
- Open access
- green
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