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Synthesis and evaluation of benzothiazole-triazole and benzothiadiazole-triazole scaffolds as potential molecular probes for amyloid-β aggregation.
Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering. Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada(1);Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, MG, Brazil(3);CAPES Foundation, Ministry of Education of Brazil, 70040-020 Brasília, DF, Brazil.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
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2017 (English)In: New Journal of Chemistry, ISSN 1144-0546, E-ISSN 1369-9261, Vol. 41, no 4, p. 8p. 1566-1573Article in journal (Refereed) Published
Abstract [en]

Small-molecule ligands that bind to misfolded protein aggregates are essential tools for the study and detection of pathological hallmarks in neurodegenerative disorders, such as Alzheimer's disease (AD). In the present study, three compounds (one benzothiazole-triazole, L1, and two benzothiadiazole-triazoles, L2 and L3) were synthesized via a modular approach (azide–alkyne cycloaddition) and evaluated as potential ligands for amyloid-β (Aβ) aggregates. The binding to amyloid-like fibrils, generated from recombinant Aβ1–42, were studied and the binding specificity to amyloid deposits was evaluated in brain sections from transgenic mice with AD pathology. All three derivatives showed significant reduced emission in the presence of recombinant Aβ1–42 amyloid fibrils. In addition, the observed binding to Aβ deposits in tissue sections suggests that the benzothiazole-triazole and benzothiadiazole-triazole structures are promising molecular scaffolds that can be modified for binding to specific protein aggregates. [ABSTRACT FROM AUTHOR]

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2017. Vol. 41, no 4, p. 8p. 1566-1573
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Other Basic Medicine
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URN: urn:nbn:se:liu:diva-135364DOI: 10.1039/c6nj01703gISI: 000395092600019OAI: oai:DiVA.org:liu-135364DiVA, id: diva2:1081314
Available from: 2017-03-13 Created: 2017-03-13 Last updated: 2018-01-13

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