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.

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Record number 434249
Title Conformational and self-assembly properties of cyclic lipodepsipeptides of the viscosin group
Author(s) Sinnaeve, D.; Geudens, N.; Vleeschouwer, M. De; Feher, K.; Rokni-Zadeh, H.; Raaijmakers, J.M.; Mot, R. De; Madder, A.; Martins, J.C.
Source Journal of Peptide Science 18 (2012). - ISSN 1075-2617 - p. S160 - S161.
Department(s) Laboratory of Phytopathology
Publication type Abstract in scientific journal or proceedings
Publication year 2012
Abstract Cyclic lipodepsipeptides (CLPs) are secondary metabolites produced by various bacteria, most prominently Bacillus and Pseudomonas. These often display potential antimicrobial properties, frequently ascribed to the ability to disrupt cellular membranes or form ion-pores. CLPs are a structurally diverse group of molecules always consisting of an oligopeptide chain cyclized by a lacton bond and a fatty acid moiety. They are divided into several groups based on sequence similarity. One such group is the viscosin group, which contains CLPs produced by Pseudomonas that all feature nine amino acids and a conserved sequence pattern of hydrophobic and hydrophilic residues.1 Recently, we have extensively described the self-assembly properties of one viscosin group member, pseudodesmin A.2,3 We have shown that in non-polar organic solvents this CLP forms anisotropic supramolecular structures of unrestricted size, reminiscent of the ability to form ionpores in the non-polar cellular membrane environment. Here, we report on how the most prominent structural variations within the viscosin group affect the conformation and self-assembly properties. Since the well-defined monomer conformation of pseudodesmin A is key to this self-assembly, the most striking variation within the viscosin group is the variability of the Leu5 stereochemistry. For the first time, a conformational study will be reported for CLPs featuring an L-Leu5 residue, such as viscosin and viscosinamide. The results of this study contribute to a deeper understanding of the structure-function relationship of CLPs in general.
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