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.


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)

DOI: 10.1002/psc.924

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)

DOI: 10.1016/j.bmcl.2007.01.075

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)

DOI: 10.1529/biophysj.105.063040

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)

DOI: 10.1002/cbic.200500095

last changes 09.03.2013, Peter Schmieder