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000003797 0247_ $$2DOI$$a10.1002/cmdc.200800289
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000003797 084__ $$2WoS$$aChemistry, Medicinal
000003797 084__ $$2WoS$$aPharmacology & Pharmacy
000003797 1001_ $$0P:(DE-HGF)0$$avan Groen, T.$$b0
000003797 245__ $$aIn vitro and in vivo staining characteristics of small, fluorescent, Aß42 binding D-enantiomeric peptides in transgenic AD mouse models
000003797 260__ $$aWeinheim [u.a.]$$bWiley-VCH$$c2009
000003797 300__ $$a276 - 282
000003797 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000003797 500__ $$aThis work was supported by a grant from the Volkswagen-Stiftung to D.W. (1/82 649).
000003797 520__ $$aOne of the characteristic pathological hallmarks of Alzheimer's disease (AD) are neuritic plaques that consist of amyloid peptide (Abeta). To improve diagnosis and treatment evaluation, neuroimaging tools that make use of Abeta-binding ligands to visualise amyloid plaques are being developed. We investigate the in vitro and in vivo characteristics of a series of three D-enantiomeric peptides (D1-D3) that were developed to specifically bind amyloid beta1-42 (Abeta42) in the brains of transgenic AD-model mice. We stained brain sections of the mice, injected and infused the mice with these small D-peptides, and examined their staining of Abeta42 in the brain. The experiments demonstrate that the D-peptides label all plaques that contain Abeta42 in the brain. In contrast, diffuse amyloid beta deposits (which do not contain Abeta42) are not stained by any of the D-peptides. The in vivo and in vitro studies demonstrate that the D-peptides label all Abeta42 in the brain, and none of the D-peptides causes inflammation or is taken up by astrocytes or microglia. Furthermore, long-term infusion of the peptides does not cause inflammation. Together, this demonstrates that these D-peptides might be suitable for use as molecular probes to measure Abeta plaque load in the living brain for early diagnosis of Alzheimer's disease, or to monitor Abeta42 plaque load during disease progression or during treatment.
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000003797 65320 $$2Author$$aaggregation
000003797 65320 $$2Author$$aAlzheimer's disease
000003797 65320 $$2Author$$aamyloid plaques
000003797 65320 $$2Author$$abiotechnology
000003797 65320 $$2Author$$apeptides
000003797 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000003797 650_2 $$2MeSH$$aAmino Acid Sequence
000003797 650_2 $$2MeSH$$aAmyloid beta-Peptides: chemistry
000003797 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000003797 650_2 $$2MeSH$$aAnimals
000003797 650_2 $$2MeSH$$aDisease Models, Animal
000003797 650_2 $$2MeSH$$aFluorescent Dyes: chemistry
000003797 650_2 $$2MeSH$$aMice
000003797 650_2 $$2MeSH$$aMice, Transgenic
000003797 650_2 $$2MeSH$$aPeptide Fragments: chemistry
000003797 650_2 $$2MeSH$$aPeptide Fragments: metabolism
000003797 650_2 $$2MeSH$$aPeptides: metabolism
000003797 650_2 $$2MeSH$$aProtein Binding
000003797 650_2 $$2MeSH$$aStereoisomerism
000003797 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides
000003797 650_7 $$00$$2NLM Chemicals$$aFluorescent Dyes
000003797 650_7 $$00$$2NLM Chemicals$$aPeptide Fragments
000003797 650_7 $$00$$2NLM Chemicals$$aPeptides
000003797 650_7 $$00$$2NLM Chemicals$$aamyloid beta-protein (1-42)
000003797 650_7 $$2WoSType$$aJ
000003797 7001_ $$0P:(DE-HGF)0$$aKadish, I.$$b1
000003797 7001_ $$0P:(DE-HGF)0$$aWiesehan, K.$$b2
000003797 7001_ $$0P:(DE-Juel1)VDB65869$$aFunke, S. A.$$b3$$uFZJ
000003797 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
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