Antimicrobial peptides: Structure of antimicrobial peptides bound to detergent micells |
The widespread phenomenon of multidrug resistance in bacteria has necessitated the search for new antimicrobial substances. About 500 naturally occuring antimicrobial peptides are known that could provide a starting point for the development of new drugs. They exihibit a large variety of sequences, secondary structures and contain L- as well as D- and unnatural amino acids. Several hypotheses regarding their mechanism of action have been presented. The goal of this project is to obtain three-dimensional structures of small anitmicrobial peptides in a membrane mimicking environment using solution state NMR since only with structural information at hand a detailed picture of the mechanism can be developed. |
Publications |
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C. Appelt; A. Wessolowski; M. Dathe; P. Schmieder*; "Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity"; J. Pept. Sci. 14, 524-527 (2008) |
C. Appelt; A.K. Schrey; J.A. Söderhäll; P. Schmieder*; "Design of antimicrobial compounds based on peptide structures"; Bioorg. Med. Chem. Lett. 17, 2334-2337 (2007) |
C. Appelt; F. Eisenmenger; R. Kühne; P. Schmieder; J.A. Söderhäll*; "Interaction of the antimicrobial peptide cyclo(RRWWRF) with membranes by molecular dynamics simulations"; Biophys. J. 89, 2296-2306 (2005) |
C. Appelt; A. Wessolowski; J. A. Söderhäll; M. Dathe; P. Schmieder*; "Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogs in solution and bound to detergent micelles"; ChemBioChem 6, 1654-1662 (2005) |
last changes 09.03.2013, Peter Schmieder