%0 Journal Article
%A Funke, S.A.
%A Liu, H.
%A Sehl, T.
%A Bartnik, D.
%A Brener, O.
%A Nagel-Steger, L.
%A Wiesehan, K.
%A Willbold, D.
%T Identification and characterization of an Aß; oligomer precipitating peptide that may be useful to explore gene therapeutic approaches to Alzheimer's disease
%J Rejuvenation research
%V 15
%@ 1549-1684
%C Larchmont, NY
%I Liebert
%M PreJuSER-20882
%P 144 - 147
%D 2012
%Z The authors gratefully acknowledge support from the "Helmholtz-CSC (China Scholarship Council) Junior Scientists Exchange Program" for Hongmei Liu.
%X A key feature of Alzheimer disease (AD) is the pathologic self-association of the amyloid-β (Aβ) peptide, leading to the formation of diffusible toxic Aβ oligomers and extracellular amyloid plaques. Next to extracellular Aβ, intraneuronal Aβ has important pathological functions in AD. Agents that specifically interfere with the oligomerization processes either outside or inside of neurons are highly desired for the elucidation of the pathologic mechanisms of AD and might even pave the way for new AD gene therapeutic approaches. Here, we characterize the Aβ binding peptide L3 and its influence on Aβ oligomerization in vitro. Preliminary studies in cell culture demonstrate that stably expressed L3 reduces cell toxicity of externally added Aβ in neuroblastoma cells.
%K Alzheimer Disease: genetics
%K Alzheimer Disease: therapy
%K Amyloid beta-Peptides: chemistry
%K Animals
%K Cell Line, Tumor
%K Centrifugation, Density Gradient
%K Disease Models, Animal
%K Gene Therapy: methods
%K Humans
%K Mice
%K Nephelometry and Turbidimetry
%K Neurons: metabolism
%K Peptides: chemistry
%K Sequence Analysis, DNA
%K Thiazoles: chemistry
%K Amyloid beta-Peptides (NLM Chemicals)
%K Peptides (NLM Chemicals)
%K Thiazoles (NLM Chemicals)
%K thioflavin T (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:22533419
%U <Go to ISI:>//WOS:000303383600008
%R 10.1089/rej.2011.1262
%U https://juser.fz-juelich.de/record/20882