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Poly-N-methylated Amyloid β-Peptide (Aβ) C-Terminal Fragments Reduce Aβ Toxicity in Vitro and in Drosophila melanogaster
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
Department of Anatomy, Physiology, and Biochemistry, Swedish University of Agricultural Sciences.
Department of Anatomy, Physiology, and Biochemistry, Swedish University of Agricultural Sciences.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
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2009 (English)In: Journal of Medicinal Chemistry, ISSN 0022-2623, E-ISSN 1520-4804, Vol. 52, no 24, 8002-8009 p.Article in journal (Refereed) Published
Abstract [en]

Alzheimer’s disease (AD), an age related neurodegenerative disorder, threatens to become a major health-economic problem. Assembly of 40- or 42-residue amyloid β-peptides (Aβ) into neurotoxic oligo-/polymeric β-sheet structures is an important pathogenic feature in AD, thus, inhibition of this process has been explored to prevent or treat AD. The C-terminal part plays an important role in Aβ aggregation, but most Aβ aggregation inhibitors have targeted the central region around residues 16−23. Herein, we synthesized hexapeptides with varying extents of N-methylation based on residues 32−37 of Aβ, to target its C-terminal region. We measured the peptides' abilities to retard β-sheet and fibril formation of Aβ and to reduce Aβ neurotoxicity. A penta-N-methylated peptide was more efficient than peptides with 0, 2, or 3 N-methyl groups. This penta-N-methylated peptide moreover increased life span and locomotor activity in Drosophila melanogaster flies overexpressing human Aβ1−42.

Place, publisher, year, edition, pages
2009. Vol. 52, no 24, 8002-8009 p.
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Chemical Sciences
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URN: urn:nbn:se:uu:diva-112210DOI: 10.1021/jm901092hISI: 000272712100016PubMedID: 19908889OAI: oai:DiVA.org:uu-112210DiVA: diva2:285408
Available from: 2010-01-11 Created: 2010-01-11 Last updated: 2017-12-12Bibliographically approved

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Gogoll, Adolf

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