Vejleder: Beate Klösgen
Deltagerantal: 1 studerende
Bacterial resistance against antibiotics is unavoidably driven by regular bio-evolution. This imposes treatment problems and new antibiotics targeting immutable structures are needed. E.g., the bacterial cell wall is a target surface of antibiotic attack, with the human anti-inflammatory peptide LL-37 being as a generic candidate.
The interaction of the peptide, and selected fragments, on model lipid interfaces was studied by diverse methods including Langmuir compression combined with GIXD (grazing incidence X-ray diffraction). The results report on the adsorption and insertion affinity of the peptide to the interface and the change of in-plane crystallographic order upon the interaction.
The bachelor (or master) project shall contribute by analysis of recent GIXD data, collected during winter 2019/2020 in experiments at beamline P08 (PetraIII). The data involve the development of lateral structures during Langmuir compression. The project will focus on analysis of existing data. The student not conduct actual experiments, but instead learn about crystallography in 2D, and how to use professional software for the data processing, from data reduction to crystallographic analysis. The results shall be compared to older results collected in previous beamtimes. The findings shall be assembled and discussed, to be filed into a thesis text.