Journal Article

FZJ-2016-01815

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity

Rudolph, S. ; Klein, A. N. ; Tusche, M.FZJ* ; Schlosser, C. ; Elfgen, A.FZJ* ; Brener, O. ; Teunissen, C. ; Gremer, L.FZJ* ; Funke, S. A. ; Kutzsche, J.FZJ* ; Willbold, D. (Corresponding author)FZJ*

2016
PLoS Lawrence, Kan.

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Please use a persistent id in citations: http://hdl.handle.net/2128/9910  doi:10.1371/journal.pone.0147470

Abstract: Alzheimer´s disease is the most prominent type of dementia and currently no causative treatment is available. According to recent studies, oligomeric species of the amyloid beta (Aβ) peptide appear to be the most toxic Aβ assemblies. Aβ monomers, however, may be not toxic per se and may even have a neuroprotective role. Here we describe a competitive mirror image phage display procedure that allowed us to identify preferentially Aβ1–42 monomer binding and thereby stabilizing peptides, which destabilize and thereby eliminate toxic oligomer species. One of the peptides, called Mosd1 (monomer specific d-peptide 1), was characterized in more detail. Mosd1 abolished oligomers from a mixture of Aβ1–42 species, reduced Aβ1–42 toxicity in cell culture, and restored the physiological phenotype in neuronal cells stably transfected with the gene coding for human amyloid precursor protein.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)

Appears in the scientific report 2016

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Database coverage:
; ; ; ; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record

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