Hauptseite > Publikationsdatenbank > Inhibition of cytotoxicity and amyloid fibril formation by a D-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide > print

001     338
005     20200731122044.0
024 7 _ |a pmid:18252750
|2 pmid
024 7 _ |a 10.1093/protein/gzm054
|2 DOI
024 7 _ |a WOS:000254295200003
|2 WOS
024 7 _ |a altmetric:21800179
|2 altmetric
024 7 _ |a 2128/25408
|2 Handle
037 _ _ |a PreJuSER-338
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biotechnology & Applied Microbiology
100 1 _ |a Wiesehan, K.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB15437
245 _ _ |a Inhibition of cytotoxicity and amyloid fibril formation by a D-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide
260 _ _ |a Oxford
|b Oxford Univ. Press
|c 2008
300 _ _ |a 241 - 246
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Protein Engineering Design & Selection
|x 1741-0126
|0 19161
|v 21
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Alzheimer'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.
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|c P33
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: antagonists & inhibitors
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: metabolism
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: toxicity
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cell Death: drug effects
650 _ 2 |2 MeSH
|a Cytotoxins: antagonists & inhibitors
650 _ 2 |2 MeSH
|a Cytotoxins: metabolism
650 _ 2 |2 MeSH
|a Cytotoxins: toxicity
650 _ 2 |2 MeSH
|a Microscopy, Electron
650 _ 2 |2 MeSH
|a PC12 Cells
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Peptides: metabolism
650 _ 2 |2 MeSH
|a Peptides: pharmacology
650 _ 2 |2 MeSH
|a Polymers: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Secondary: drug effects
650 _ 2 |2 MeSH
|a Rats
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 2 |2 MeSH
|a Substrate Specificity
650 _ 2 |2 MeSH
|a Thiazoles: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Cytotoxins
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Polymers
650 _ 7 |0 0
|2 NLM Chemicals
|a Thiazoles
650 _ 7 |0 2390-54-7
|2 NLM Chemicals
|a thioflavin T
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a A beta
653 2 0 |2 Author
|a aggregation
653 2 0 |2 Author
|a Alzheimer's disease
653 2 0 |2 Author
|a cytotoxicity
653 2 0 |2 Author
|a D-amino acid peptide
700 1 _ |a Stöhr, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Nagel-Steger, K.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a van Groen, T.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Riesner, D.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 5
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1093/protein/gzm054
|g Vol. 21, p. 241 - 246
|p 241 - 246
|q 21<241 - 246
|0 PERI:(DE-600)1466729-0
|t Protein engineering design and selection
|v 21
|y 2008
|x 1741-0126
856 7 _ |u http://dx.doi.org/10.1093/protein/gzm054
856 4 _ |u https://juser.fz-juelich.de/record/338/files/gzm054.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/338/files/gzm054.pdf?subformat=pdfa
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