|Antimicrobial peptides: Structure of antimicrobial
peptides bound to detergent micells
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)
| 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
| 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