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Form and function : structural variations of natural cyclic lipodepsipeptides

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Abstract
Cyclic lipodepsipeptides (CLPs) are non-ribosomal bacterial peptides, which exhibit antagonistic activity against several bacterial and fungal species. CLPs increasingly attract attention in the field of crop protection, where they serve as valuable alternatives to chemical pesticides. A full understanding of their conformation and membrane interactions is essential to elucidate the exact working mechanism of these molecules. [1 – 4] CLPs consist of an oligopeptide chain containing both D- and L-amino acids which forms a cyclic structure by means of an ester (depsi) bond. Depending on the bacterial producer strain, there is a very large range of different CLPs that are produced. Therefore, the CLPs are classified into several groups according to oligopeptide chain length, size of the cyclic fragment and sequence similarity. CLPs adopt a well-defined amphipathic conformation, as determined by liquid-state NMR and X-ray crystallography [2, 3]. Based on a detailed analysis of individual peptide sequences, similar structural features can be found across different CLP groups. We hypothesize the existence of “super groups” with fixed structural motifs, founded on clear differences and similarities in sequence composition and length. This proposal will be discussed in the presentation by confronting the NMR-derived three-dimensional conformations of several CLPs belonging to different groups, including viscosins, orfamides, amphisins and xantholysins. These structural motifs potentially have predictive capabilities: they will allow to predict the three-dimensional structure of new CLPs and new CLP groups, or predict the effect of certain structural modification introduced by solid-phase peptide synthesis. [5] Furthermore, they can potentially be linked to a differential working mechanism across the different super groups. References 1. Geudens N., M.N. Nasir, et al., Biochimica Biophysica Acta, 2017, 1859, 331-339 2. Geudens N., M. De Vleeschouwer, et al., ChemBioChem, 2014, 15, 2736-2746 3. Sinnaeve, D., C. Michaux, et al., Tetrahedron, 2009, 65(21): 4173-4181 4. Sinnaeve, D., P. M. Hendrickx, et al., Chemistry - A European Journal, 2009, 15(46): 12653-12662 5. De Vleeschouwer, M., D. Sinnaeve, et al., Chemistry - A European Journal, 2014, 20, 7766-7775

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Chicago
Geudens, Niels, Benjámin Kovács, Vic De Roo, Feyisara Eyiwumi Oni, Maarten Ghequire, René De Mot, Monica Höfte, and José Martins. 2018. “Form and Function : Structural Variations of Natural Cyclic Lipodepsipeptides.” In Belgian Peptide Group, 4th Meeting, Abstracts.
APA
Geudens, N., Kovács, B., De Roo, V., Oni, F. E., Ghequire, M., De Mot, R., Höfte, M., et al. (2018). Form and function : structural variations of natural cyclic lipodepsipeptides. Belgian Peptide Group, 4th Meeting, Abstracts. Presented at the 4th Belgian Peptide Group meeting.
Vancouver
1.
Geudens N, Kovács B, De Roo V, Oni FE, Ghequire M, De Mot R, et al. Form and function : structural variations of natural cyclic lipodepsipeptides. Belgian Peptide Group, 4th Meeting, Abstracts. 2018.
MLA
Geudens, Niels et al. “Form and Function : Structural Variations of Natural Cyclic Lipodepsipeptides.” Belgian Peptide Group, 4th Meeting, Abstracts. 2018. Print.
@inproceedings{8591046,
  abstract     = {Cyclic lipodepsipeptides (CLPs) are non-ribosomal bacterial peptides, which exhibit antagonistic activity against several bacterial and fungal species. CLPs increasingly attract attention in the field of crop protection, where they serve as valuable alternatives to chemical pesticides. A full understanding of their conformation and membrane interactions is essential to elucidate the exact working mechanism of these molecules. [1 -- 4]
CLPs consist of an oligopeptide chain containing both D- and L-amino acids which forms a cyclic structure by means of an ester (depsi) bond. Depending on the bacterial producer strain, there is a very large range of different CLPs that are produced. Therefore, the CLPs are classified into several groups according to oligopeptide chain length, size of the cyclic fragment and sequence similarity. 
CLPs adopt a well-defined amphipathic conformation, as determined by liquid-state NMR and X-ray crystallography [2, 3]. Based on a detailed analysis of individual peptide sequences, similar structural features can be found across different CLP groups. We hypothesize the existence of {\textquotedblleft}super groups{\textquotedblright} with fixed structural motifs, founded on clear differences and similarities in sequence composition and length. This proposal will be discussed in the presentation by confronting the NMR-derived three-dimensional conformations of several CLPs belonging to different groups, including viscosins, orfamides, amphisins and xantholysins.
These structural motifs potentially have predictive capabilities: they will allow to predict the three-dimensional structure of new CLPs and new CLP groups, or predict the effect of certain structural modification introduced by solid-phase peptide synthesis. [5] Furthermore, they can potentially be linked to a differential working mechanism across the different super groups.
References
1. Geudens N., M.N. Nasir, et al., Biochimica Biophysica Acta, 2017, 1859, 331-339
2. Geudens N., M. De Vleeschouwer, et al., ChemBioChem, 2014, 15, 2736-2746
3. Sinnaeve, D., C. Michaux, et al., Tetrahedron, 2009, 65(21): 4173-4181
4. Sinnaeve, D., P. M. Hendrickx, et al., Chemistry - A European Journal, 2009, 15(46): 12653-12662
5. De Vleeschouwer, M., D. Sinnaeve, et al., Chemistry - A European Journal, 2014, 20, 7766-7775},
  author       = {Geudens, Niels and Kov{\'a}cs, Benj{\'a}min and De Roo, Vic and Oni, Feyisara Eyiwumi and Ghequire, Maarten and De Mot, Ren{\'e} and H{\"o}fte, Monica and Martins, Jos{\'e}},
  booktitle    = {Belgian Peptide Group, 4th Meeting, Abstracts},
  language     = {eng},
  location     = {Brussels, Belgium},
  title        = {Form and function : structural variations of natural cyclic lipodepsipeptides},
  year         = {2018},
}