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The peptide sequence KLVFF resembles the hydrophobic core of the Aβ peptide known to form amyloid plaques in Alzheimer’s disease. Starting from its retro-inverso peptide, we have synthesized three generations of peptidomimetics. Step by step natural amino acids have been replaced by aromatic building blocks accessible from the Pd-catalyzed Catellani reaction. The final compound 18is stable against proteolytic decay and largely prevents the aggregation of Aβ1–42over extended periods of time. The activity of the new inhibitors was tested first by fluorescence correlation spectroscopy. For closer examination of compound 18, additional techniques were also applied: laser-induced liquid bead ion desorption mass spectrometry, confocal laser scanning microscopy, thioflavin T fluorescence, and gel electrophoresis. Compound 18not only retards the aggregation of chemically synthesized Aβ but also can partially dissolve the oligomeric structures. Thioflavin binding mature fibrils, however, seem to resist the inhibitor.

This work deals with the application of ozonated water for the BEOL stripping of DUV-resists. For this purpose analytical techniques for the quantification of molecular O3 in the water as well as methods for the non-destructive analysis of resists on wafers have been studied. The aim is to be able to determine the concentrations of O3, its decomposition, under the influence of various parameters, and to correlate these data with the polymer structure of the resist on the wafer and the efficiency of resist removal.