Marie-Charlotte Lechner

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Ongoing clinical trials are exploring anticancer approaches based on signaling by TRAIL, a ligand for the cell death receptors DR4 and DR5. In this study, we report on the selective apoptotic effects of multivalent DR5 binding peptides (TRAIL(mim/DR5)) on cancer cells in vitro and in vivo. Surface plasmon resonance revealed up to several thousand-fold(More)
DR4 (Death Receptor 4) and DR5 (Death Receptor 5) are two potential targets for cancer therapy due to their ability to trigger apoptosis of cancer cells, but not normal ones, when activated by their cognate ligand TRAIL (TNF related apoptosis-inducing ligand). Therapies based on soluble recombinant TRAIL or agonist antibodies directed against one of the(More)
Cyclic peptides containing redox-stable thioether bridges might provide a useful alternative to disulfide-bridged bioactive peptides. We report the effect of replacing the disulfide bridge with a lanthionine linkage in a 16-mer cyclic peptide that binds to death receptor 5 (DR5, TRAIL-R2). Upon covalent oligomerisation, the disulfide-bridged peptide has(More)
The title compound, C(10)H(15)NO(4), also known as N-tert-butyl-oxycarbonyl-allohydr-oxy-l-proline lactone, is quite similar to N-acetyl-allohydr-oxy-l-proline lactone [Lenstra, Petit & Geise (1979 ▶). Cryst. Struct. Commun. 8, 1023-1029], whereby both carbonyl groups point roughly in the same direction because of the trans conformation of the peptide bond.
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