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Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore
Swiss Fed Inst Technol, Switzerland.
Univ Zurich, Switzerland.
Swiss Fed Inst Technol, Switzerland.
Univ Zurich, Switzerland.
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2018 (English)In: ACS Chemical Neuroscience, ISSN 1948-7193, E-ISSN 1948-7193, Vol. 9, no 3, p. 475-481Article in journal (Refereed) Published
Abstract [en]

Luminescent conjugated polythiophenes bind to amyloid proteins with high affinity. Their fluorescence properties, which are modulated by the detailed conformation in the bound state, are highly sensitive to structural features of the amyloid. Polythiophenes therefore represent diagnostic markers for the detection and differentiation of pathological amyloid aggregates. 560 We clarify the binding site and mode of two different polythiophenes to fibrils of the prion domain of the HET-s protein by solid-state NMR and correlate these findings with their fluorescence properties. We demonstrate how amyloid dyes recognize distinct binding sites with specific topological features. Regularly spaced surface charge patterns and well-accessible grooves on the fibril surface define the pharmacophore of the amyloid, which in turn determines the binding mode and fluorescence wavelength of the polythiophene.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018. Vol. 9, no 3, p. 475-481
Keywords [en]
Amyloid; pharmacophore; luminescent conjugated polythiophenes; diagnostic marker; fluorescence; solid-state NMR
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-147430DOI: 10.1021/acschemneuro.7b00397ISI: 000428356500012PubMedID: 29178774Scopus ID: 2-s2.0-85037681655OAI: oai:DiVA.org:liu-147430DiVA, id: diva2:1206545
Note

Funding Agencies|Swiss National Science Foundation [200020_159707, 200020_146757, 200020_147660]; French ANR [ANR-14-CE09-0024B]; European Research Council [ERC: 670958]

Available from: 2018-05-17 Created: 2018-05-17 Last updated: 2018-05-22Bibliographically approved

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Hammarström, Per

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CiteExportLink to record
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  • apa
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