The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers
| Autor: | Drew Nahirney, John C. Vederas, Marek Duszyk, Leah A. Martin-Visscher, Xiandi Gong |
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| Rok vydání: | 2009 |
| Předmět: |
Anions
Pore formation Lipid Bilayers Antimicrobial peptides Biophysics Biology Peptides Cyclic Biochemistry Ion Channels Membrane Potentials Lipid bilayer 03 medical and health sciences Bacteriocins Bacteriocin Ion channel 030304 developmental biology Membrane potential 0303 health sciences 030306 microbiology Membrane Bacterial toxin Cell Biology biology.organism_classification Antimicrobial 3. Good health Antimicrobial peptide Bacteria |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788:1797-1803 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2009.05.008 |
| Popis: | Bacterial resistance to conventional antibiotics is a major challenge in controlling infectious diseases and has necessitated the development of novel approaches in antimicrobial therapy. One such approach is the use of antimicrobial peptides, such as the bacterially produced bacteriocins. Carnocyclin A (CclA) is a 60-amino acid circular bacteriocin produced by Carnobacterium maltaromaticum UAL307 that exhibits potent activity against many Gram-positive bacteria. Lipid bilayer and single channel recording techniques were applied to study the molecular mechanisms by which CclA interacts with the lipid membrane and exerts its antimicrobial effects. Here we show that CclA can form ion channels with a conductance of 35 pS in 150 mM NaCl solution. This channel displays a linear current–voltage relationship, is anion-selective, and its activation is strongly voltage-dependent. The formation of ion channels by CclA is driven by the presence of a negative membrane potential and may result in dissipation of membrane potential. Carnocyclin A's unique functional activities as well as its circular structure make it a potential candidate for developing novel antimicrobial drugs. |
| Databáze: | OpenAIRE |
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