Control of Protein Folding and Protein Self Assembling through Fluorine-Specific Interactions (A04)

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A4|Koksch deals with the segregation properties of fluorinated groups with respect to protein folding. For this, fluorinated amino acids will be incorporated into beta-sheet domains of proteins. Furthermore, the formation of networks between fluorinated derivatives of the serine-protease-inhibitor BPTI with the proteases β-trypsin and α-chymotrypsin as well as the protein-inhibitor-complex barnase/barstar are investigated. Finally, the abil-ity for self-assembly of novel, highly fluorinated model peptides and their interaction with model membranes (SDS, POPC/POPG) and intact cells is studied.