Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 414645
Title Model membrane studies for characterization of different antibiotic activities of lipopeptides from Pseudomonas
Author(s) Reder-Christ, K.; Schmidt, Y.; Dörr, M.; Sahl, H.G.; Raaijmakers, J.; Gross, H.; Josten, M.; Bendas, G.
Source Biochimica et Biophysica Acta. Biomembranes 1818 (2012)3. - ISSN 0005-2736 - p. 566 - 573.
Department(s) Laboratory of Phytopathology
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) red-blood-cells - versatile soil bacterium - complete genome sequence - bilayer-lipid membranes - syringae pv. syringae - syringomycin-e - mycobacterium-smegmatis - cyclic lipodepsipeptides - biosensor techniques - fluorescens
Abstract Lipopeptides (LPs) are a structurally diverse class of amphipathic natural products that were in the past mainly known for their surfactant properties. However, the recent discovery of their antimicrobial and cytotoxic bioactivities have fueled and renewed the interest in this compound class. Propelled by the antimicrobial potential of this compound class, in this study a range of six underinvestigated LPs from Pseudomonads were examined with respect to their antibiotic activities towards bacteria. The assays revealed that only the glycosylated lipodipeptide SB-253514, produced by Pseudomonas strain SH-C52, showed significant antibacterial activity. Since the bioactivity of LPs is commonly attributed to membrane interactions, we analyzed the molecular interactions between the LPs and bacteria-like lipid model membranes in more detail via complementary biophysical approaches. Application of the quartz crystal microbalance (QCM) showed that all LPs possess a high binding affinity towards the model membranes. Despite their similar membrane affinity, monolayer studies displayed different tendencies of LPs to incorporate into the membrane. The degree of membrane incorporation could be correlated with specific structural features of the investigated LPs, such as distance between the peptidic macrocycle and the fatty acid, but did not fully reflect their respective antibacterial activity. Cyclic voltammetry (CV) experiments further demonstrated that SB-253514 showed no membrane permeabilization effects at inhibitory concentrations. Collectively, these results suggests that the antibacterial activity of SB-253514 cannot be explained by an unspecific detergent-like mechanism generally proposed for amphiphilic molecules but instead appears to occur via a defined structural target.
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