Author
A. A. Lugovski
Bio: A. A. Lugovski is an academic researcher from Belarusian State University. The author has contributed to research in topics: Benzothiazole & Thioflavin. The author has an hindex of 1, co-authored 2 publications receiving 1 citations.
Topics: Benzothiazole, Thioflavin
Papers
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TL;DR: In this article, a modification of the Thioflavin T (ThT) structure via introduction of methyl and methoxy groups was described, and the effects of the substituents on fluorescence were investigated.
Abstract: New fluorescent molecular rotors (FMRs) were developed by modification of the Thioflavin T (ThT) structure via introduction of methyl and methoxy groups. Effects of the substituents on fluorescence...
1 citations
01 Sep 2018
TL;DR: In this paper, the benzothiazole styryl dyes that exhibit properties as molecular rotors for amyloid fibrils detection have been synthesized, which are covalently bounded to polyethylene glycols with an average molecular weight of 300 g/mol.
Abstract: New benzothiazole styryl dyes that exhibit properties as molecular rotors for amyloid fibrils detection have been synthesized. Synthesized dyes are covalently bounded to polyethylene glycols with an average molecular weight of 300 g/mol. Photophysical investigation and quantum-chemical calculations for synthesized dyes were carried out. Presence of amyloid fibrils in the solution leads to increase in fluorescence intensity of dyes by almost two orders of magnitude. It is shown that compounds can be used as effective fluorescent biosensors for amyloid fibrils detection.
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TL;DR: The properties of the derivatives provide new insights into the relationship between chemical structure and function of benzothiazole probes and their abilities to perform super-resolution imaging of α-synuclein fibrils with localisation precisions of ~16 nm.
Abstract: The benzothiazolium salt, Thioflavin T (ThT), has been widely adopted as the "gold-standard" fluorescent reporter of amyloid in vitro. Its properties as a molecular rotor result in a large-scale (∼1000-fold) fluorescence turn-on upon binding to β-sheets in amyloidogenic proteins. However, the complex photophysics of ThT combined with the intricate and varied nature of the amyloid binding motif means these interactions are poorly understood. To study this important class of fluorophores, we present a detailed photophysical characterization and comparison of a novel library of 12 ThT-inspired fluorescent probes for amyloid protein (PAPs), where both the charge and donor capacity of the heterocyclic and aminobenzene components have been interrogated, respectively. This enables direct photophysical juxtaposition of two structural groups: the neutral "PAP" (class 1) and the charged "mPAP" fluorophores (class 2). We quantify binding and optical properties at both the bulk and single-aggregate levels with some derivatives showing higher aggregate affinity and brightness than ThT. Finally, we demonstrate their abilities to perform super-resolution imaging of α-synuclein fibrils with localization precisions of ∼16 nm. The properties of the derivatives provide new insights into the relationship between chemical structure and function of benzothiazole probes.
10 citations