Binding of Thioflavin T and Related Probes to Polymorphic Models of Amyloid-β Fibrils

Francesca Peccati, Stefano Pantaleone, Vanessa Riffet, Xavier Solans-Monfort, Julia Contreras-García, Victor Guallar, Mariona Sodupe

Research output: Contribution to journalArticleResearchpeer-review

18 Citations (Scopus)


© 2017 American Chemical Society. Alzheimer's disease is a challenge of the utmost importance for contemporary society. An early diagnosis is essential for the development of treatments and for establishing a network of support for the patient. In this light, the deposition in the brain of amyloid-β fibrillar aggregates, which is a distinctive feature of Alzheimer, is key for an early detection of this disease. In this work we propose an atomistic study of the interaction of amyloid tracers with recently published polymorphic models of amyloid-β 1-40 and 1-42 fibrils, highlighting the relationship between marker architectures and binding affinity. This work uncovers the importance of quaternary structure, and in particular of junctions between amyloid-β protofilaments, as the key areas for marker binding.
Original languageEnglish
Pages (from-to)8926-8934
JournalJournal of Physical Chemistry B
Issue number38
Publication statusPublished - 28 Sep 2017

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