Structural Analogue of Thioflavin T, DMASEBT, as a Tool for Amyloid Fibrils Study

Sulatskaya, Anna I.; Sulatsky, Maksim I.; Antifeeva, Iuliia A.; Kuznetsova, Irina М.; Turoverov, Konstantin К.

doi:10.1021/acs.analchem.8b05737

Cited by 17 publications

(8 citation statements)

References 51 publications

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“…During ThT interaction with lysozyme amyloid fibrils, we observed a slight change in the shape of the dye absorption spectrum (the appearance of a shoulder in the long-wavelength region of the spectrum) ( Figure 2(e)). When the dye binds to insulin amyloid fibrils, its absorption spectrum shifts noticeably to the long-wavelength region and changes its shape (Figure 2(e)), which is in good agreement with the results obtained by us earlier [20,45]. ThT fluorescence intensity increases more significantly when dye interacts with insulin amyloid fibrils than when it binds to lysozyme amyloid fibrils (Figure 2(f)).…”

Section: Fluorescent Probes Tht and Ans Have Different Amyloid Fibrilsupporting

confidence: 89%

Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils

Sulatsky

Sulatskaya

Povarova

et al. 2020

Prion

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Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study.

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Section: Fluorescent Probes Tht and Ans Have Different Amyloid Fibrilsupporting

confidence: 89%

Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils

Sulatsky

Sulatskaya

Povarova

et al. 2020

Prion

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“…The search for novel, more sensitive and blood-brain barrier crossing dyes for detecting the initial stages and more toxic oligomeric species involved in fibril formation in vitro, ex vivo and in vivo is still under way [43][44][45]. Nevertheless, several related structures or derivatives of both CR [46][47][48][49] and ThT [50][51][52][53] have been shown to be quite helpful for both in vitro and ex vivo identification of amyloid fibrils ( Figure 2).…”

Section: The Tinctorial Properties Of Amyloid Fibrilsmentioning

confidence: 99%

Structure and Aggregation Mechanisms in Amyloids

2020

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The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and deposition into insoluble plaques and intracellular inclusions is the hallmark of several misfolding diseases known as amyloidoses. Alzheimer′s, Parkinson′s and Huntington’s diseases are some of the approximately 50 amyloid diseases described to date. The identification and characterization of the molecular species critical for amyloid formation and disease development have been the focus of intense scrutiny. Methods such as X-ray and electron diffraction, solid-state nuclear magnetic resonance spectroscopy (ssNMR) and cryo-electron microscopy (cryo-EM) have been extensively used and they have contributed to shed a new light onto the structure of amyloid, revealing a multiplicity of polymorphic structures that generally fit the cross-β amyloid motif. The development of rational therapeutic approaches against these debilitating and increasingly frequent misfolding diseases requires a thorough understanding of the molecular mechanisms underlying the amyloid cascade. Here, we review the current knowledge on amyloid fibril formation for several proteins and peptides from a kinetic and thermodynamic point of view, the structure of the molecular species involved in the amyloidogenic process, and the origin of their cytotoxicity.

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“…The study of amyloid aggregation should always be complemented with various other biophysical techniques, including circular dichroism (CD) and Fourier transfer infrared spectroscopy (FTIR) for secondary structure characterisation, and AFM and EM for fibril imaging. Several derivatives of ThT have been developed for in vivo detection of amyloid fibrils in the organs and tissues of live patients [46,47]. Amyloid probes also include luminescent conjugated oligothiophenes, which are fluorescent amyloid ligands that can report on the fibrillar conformation, facilitating the in vitro and ex vivo analysis of polymorphism [48,49].…”

Section: Accepted Manuscriptmentioning

confidence: 99%