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000000338 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000338 084__ $$2WoS$$aBiotechnology & Applied Microbiology
000000338 1001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b0$$uFZJ
000000338 245__ $$aInhibition of cytotoxicity and amyloid fibril formation by a D-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide
000000338 260__ $$aOxford$$bOxford Univ. Press$$c2008
000000338 300__ $$a241 - 246
000000338 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000338 440_0 $$019161$$aProtein Engineering Design & Selection$$v21$$x1741-0126
000000338 500__ $$aRecord converted from VDB: 12.11.2012
000000338 520__ $$aAlzheimer's disease (AD) is a progressive neurodegenerative disorder. The 'amyloid cascade hypothesis' assigns the amyloid-beta-peptide (Abeta) a central role in the pathogenesis of AD. Although it is not yet established, whether the resulting Abeta aggregates are the causative agent or just a result of the disease progression, polymerization of Abeta has been identified as a major feature during AD pathogenesis. Inhibition of the Abeta polymer formation, thus, has emerged as a potential therapeutic approach. In this context, we identified peptides consisting of d-enantiomeric amino acid peptides (d-peptides) that bind to Abeta. D-peptides are known to be more protease resistant and less immunogenic than the respective L-enantiomers. Previously, we have shown that a 12mer D-peptide specifically binds to Abeta amyloid plaques in brain tissue sections from former AD patients. In vitro obtained binding affinities to synthetic Abeta revealed a K(d) value in the submicromolar range. The aim of the present study was to investigate the influence of this d-peptide to Abeta polymerization and toxicity. Using cell toxicity assays, thioflavin fluorescence, fluorescence correlation spectroscopy and electron microscopy, we found a significant effect of the d-peptide on both. Presence of D-peptides (dpep) reduces the average size of Abeta aggregates, but increases their number. In addition, Abeta cytotoxicity on PC12 cells is reduced in the presence of dpep.
000000338 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000000338 650_2 $$2MeSH$$aAmyloid beta-Peptides: antagonists & inhibitors
000000338 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000000338 650_2 $$2MeSH$$aAmyloid beta-Peptides: toxicity
000000338 650_2 $$2MeSH$$aAnimals
000000338 650_2 $$2MeSH$$aCell Death: drug effects
000000338 650_2 $$2MeSH$$aCytotoxins: antagonists & inhibitors
000000338 650_2 $$2MeSH$$aCytotoxins: metabolism
000000338 650_2 $$2MeSH$$aCytotoxins: toxicity
000000338 650_2 $$2MeSH$$aMicroscopy, Electron
000000338 650_2 $$2MeSH$$aPC12 Cells
000000338 650_2 $$2MeSH$$aPeptides: chemistry
000000338 650_2 $$2MeSH$$aPeptides: metabolism
000000338 650_2 $$2MeSH$$aPeptides: pharmacology
000000338 650_2 $$2MeSH$$aPolymers: metabolism
000000338 650_2 $$2MeSH$$aProtein Binding
000000338 650_2 $$2MeSH$$aProtein Structure, Secondary: drug effects
000000338 650_2 $$2MeSH$$aRats
000000338 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000000338 650_2 $$2MeSH$$aSubstrate Specificity
000000338 650_2 $$2MeSH$$aThiazoles: metabolism
000000338 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides
000000338 650_7 $$00$$2NLM Chemicals$$aCytotoxins
000000338 650_7 $$00$$2NLM Chemicals$$aPeptides
000000338 650_7 $$00$$2NLM Chemicals$$aPolymers
000000338 650_7 $$00$$2NLM Chemicals$$aThiazoles
000000338 650_7 $$02390-54-7$$2NLM Chemicals$$athioflavin T
000000338 650_7 $$2WoSType$$aJ
000000338 65320 $$2Author$$aA beta
000000338 65320 $$2Author$$aaggregation
000000338 65320 $$2Author$$aAlzheimer's disease
000000338 65320 $$2Author$$acytotoxicity
000000338 65320 $$2Author$$aD-amino acid peptide
000000338 7001_ $$0P:(DE-HGF)0$$aStöhr, J.$$b1
000000338 7001_ $$0P:(DE-HGF)0$$aNagel-Steger, K.$$b2
000000338 7001_ $$0P:(DE-HGF)0$$avan Groen, T.$$b3
000000338 7001_ $$0P:(DE-HGF)0$$aRiesner, D.$$b4
000000338 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b5$$uFZJ
000000338 773__ $$0PERI:(DE-600)1466729-0$$a10.1093/protein/gzm054$$gVol. 21, p. 241 - 246$$p241 - 246$$q21<241 - 246$$tProtein engineering design and selection$$v21$$x1741-0126$$y2008
000000338 8567_ $$uhttp://dx.doi.org/10.1093/protein/gzm054
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000000338 9141_ $$y2008
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000000338 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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