Analysis of membrane interactions of antibiotic peptides using ITC and biosensor measurements

Al-Kaddah, Saad and Reder-Christ, Katrin and Klocek, Gabriela and Wiedemann, Imke and Brunschweiger, Manuela and Bendas, Gerd. (2010) Analysis of membrane interactions of antibiotic peptides using ITC and biosensor measurements. Biophysical Chemistry, 152 (1-3). pp. 145-152.

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Official URL: http://edoc.unibas.ch/49528/

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The interaction of the lantibiotic gallidermin and the glycopeptide antibiotic vancomycin with bacterial membranes was simulated using mass sensitive biosensors and isothermal titration calorimetry (ITC). Both peptides interfere with cell wall biosynthesis by targeting the cell wall precursor lipid II, but differ clearly in their antibiotic activity against individual bacterial strains. We determined the binding affinities of vancomycin and gallidermin to model membranes±lipid II in detail. Both peptides bind to DOPC/lipid II membranes with high affinity (K(D) 0.30 μM and 0.27 μM). Gallidermin displayed also strong affinity to pure DOPC membranes (0.53 μM) an effect that was supported by ITC measurements. A surface acoustic wave (SAW) sensor allowed measurements in the picomolar concentration range and revealed that gallidermin targets lipid II at an equimolar ratio and simultaneously inserts into the bilayer. These results indicate that gallidermin, in contrast to vancomycin, combines cell wall inhibition and interference with the bacterial membrane integrity for potent antimicrobial activity.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Biophysical Chemistry (Seelig J)
UniBasel Contributors:Québatte, Gabriela
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:29 Nov 2017 11:22
Deposited On:29 Nov 2017 11:22

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