Vejleder: Beate Klösgen
Deltagerantal: 1 studerende
Bacterial resistance against antibiotics is unavoidably driven by regular bio-evolution. This conflicts with successful treatment such that new antibiotic drugs are needed that can target immutable structures. Here, the bacterial cell wall is a target surface of antibiotic attack, with the human anti-inflammatory peptide LL-37 being a generic candidate.
The interaction of the peptide, and selected fragments of it, on model lipid interfaces was studied by diverse methods including Langmuir compression combined with GIXD (grazing incidence X-ray diffraction) and GIXOS (grazing incidence X-ray off-specular scattering). The results report on the adsorption and insertion affinity of the peptide to the interface, on the electron density distribution at the interface and on the change of in-plane crystallographic order upon the interaction.
The bachelor (or master) project shall focus on the analysis of existing recent data, collected in x-ray scattering experiments at beamline P08 (PetraIII). The data involve the development of lateral structures during Langmuir compression. The student will not conduct actual experiments for their project at the beamline, but be invited as a hands-on student to upcoming new experiments. During their mostly computer based project work, the students will learn basics about scattering theory, as is reflectometry, x-ray fluorescence, and crystallography in 2D. They will be trained how to use professional software for the data processing, from data reduction to detailed analysis and data interpretation. The results shall be assembled and compared to older results and actual literature. The findings shall be compiled and discussed, to be filed into a thesis text.