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- W2092302307 abstract "Alzheimer's Disease (AD) is a progressive neurodegenerative disorder, affecting 20 million people world- wide. Recently there is no cure, only palliative therapies are available and the diagnostic opportunities are limited. Actually we are characterising our peptides on their binding properties to Aβ1-40, Aβ1-42 and different Aβ species (monomers, oligomers, protofibrils, fibrils and plaques) in more detail using dynamic light scattering, size exclusion chromatography, PepSpot analysis, density gradient centrifugation, surface plasmon resonance, fluorescence and electron microscopy. Using mirror image phage display, we identified two Aβ binding D-enantiomeric peptides with submicromolar binding affinity [1,2,3]. D-enantiomeric peptides are known to be less immunogenic and much more resistant to proteolysis in comparison to their respective L-enantiomers. Fluorescence labelled derivatives of the peptide D1 stain specifically Aβ plaques and leptomeningeal vessels containing Aβ from human Alzheimer brains - other amyloidoses were not stained [4]. Peptide D3 shows interesting therapeutic properties [5]. The peptide exerts strong influence on Aβ aggregation, disaggregation and cytotoxicity in vitro. In vivo, it reduces amyloid plaque load and cerebral damage of transgenic mouse models. D3 treated mice show enhanced cognitive performance in comparison to non treated controls." @default.
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- W2092302307 date "2009-07-01" @default.
- W2092302307 modified "2023-09-27" @default.
- W2092302307 title "P3-282: Investigation of low molecular weight D-enantiomeric peptides for diagnosis and therapy of Alzheimer's disease" @default.
- W2092302307 doi "https://doi.org/10.1016/j.jalz.2009.04.953" @default.
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