Molecular Mechanism of Tau Aggregation Induced by Anionic and Cationic Dyes

León, Karla I. Lira-De; García-Gutiérrez, Ponciano; Serratos, Iris N.; Palomera-Cárdenas, Marianela; Figueroa-Corona, M.D.P.; Campos-Peña, Victoria; Meraz-Ríos, Marco Antonio

doi:10.3233/jad-121765

Cited by 34 publications

(25 citation statements)

References 43 publications

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“…Fibrillar tau can thereby be recognized by dyes which interact with β-sheets, such as Congo Red and thioflavin S (52). However, at high concentrations, these dyes can induce fibrillization due to an attraction between positive charges formed in the core of PHFs and negative charges of the anionic dyes (53–55). …”

Section: Tau Oligomers Are Seeds For the Propagation Of Pathological Taumentioning

confidence: 99%

Formation and Propagation of Tau Oligomeric Seeds

Gerson¹,

Kayed²

2013

Front. Neurol.

101

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Tau misfolding and aggregation leads to the formation of neurofibrillary tangles (NFTs), which have long been considered one of the main pathological hallmarks for numerous neurodegenerative diseases known as tauopathies, including Alzheimer’s Disease (AD) and Parkinson’s Disease (PD). However, recent studies completed both in vitro and in vivo suggest that intermediate forms of tau, known as tau oligomers, between the monomeric form and NFTs are the true toxic species in disease and the best targets for anti-tau therapies. However, the exact mechanism by which the spread of pathology occurs is unknown. Evidence suggests that tau oligomers may act as templates for the misfolding of native tau, thereby seeding the spread of the toxic forms of the protein. Recently, researchers have reported the ability of tau oligomers to enter and exit cells, propagating from disease-affected regions to unaffected areas. While the mechanism by which the spreading of misfolded tau occurs has yet to be elucidated, there are a few different models which have been proposed, including cell membrane stress and pore-formation, endocytosis and exocytosis, and non-traditional secretion of protein not enclosed by a membrane. Coming to an understanding of how toxic tau species seed and spread through the brain will be crucial to finding effective treatments for neurodegenerative tauopathies.

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Section: Tau Oligomers Are Seeds For the Propagation Of Pathological Taumentioning

confidence: 99%

Formation and Propagation of Tau Oligomeric Seeds

Gerson¹,

Kayed²

2013

Front. Neurol.

101

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“… Highest scoring configurations of Flu with SBA15 obtained by docking simulations using the AutodockVina program: a) on the surface of SBA15 with Flu (SF1), the most favorable site is indicated with an arrow; b) interaction inside the pores of SBA15 with Flu (SF2); and c) on SBA15 with Flu (SF3). The 20 most favorable poses of 100 for each case were considered.…”

Section: Resultsmentioning

confidence: 99%

“…We followed the same protocol as in our previous reports . The dielectric constants were 78 and 2 for water and SBA15, respectively.…”

Section: Methodsmentioning

confidence: 99%

SBA15–Fluconazole as a Protective Approach Against Mild Steel Corrosion: Synthesis, Characterization, and Computational Studies

et al. 2018

Self Cite

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A SBA15–Fluconazole composite (SBA15‐Flu) was prepared to formulate a self‐healing coating for mild steel. The composite was obtained by dispersing SBA15 in a methanolic solution containing Fluconazole (Flu). The materials were characterized by using different techniques. Electrochemical impedance spectroscopy (EIS) was used for protective behavior evaluation of the coatings on mild steel substrates in an electrolytic solution prepared from sodium chloride and ammonium sulfate. The EIS results indicate that the inhibitor trapped in the SiO2 matrix is released when it comes into contact the aggressive solution, thus protecting the metal. To understand the inhibitor release mechanism, docking studies were used to model the SBA15‐Flu complex, which allowed us to further determine polar and non‐polar contributions to the binding free energy. An analysis of the electron density within the quantum theory of atoms in molecules and the non‐covalent interaction index frameworks were also carried out for the most favorable models of SBA15‐Flu. The results indicate that the liberation rate of the Flu molecules is mainly determined by the formation of strong O−H⋅⋅⋅O, O−H⋅⋅⋅N, and O−H⋅⋅⋅F hydrogen bonds.

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“…There are several other fluorescence dyes, including Congo red and thiazines, which have been used in histological and cell biology studies for PHF formation. At least one report stated that some of these dyes may induce tau aggregation in tissue culture cells 45 . Therefore, when choosing these compounds for amyloidogenesis kinetics studies, caution shall be practiced and that different dyes may have to be compared.…”

Section: Discussionmentioning

confidence: 99%

<em>In Vitro</em> Aggregation Assays Using Hyperphosphorylated Tau Protein

Sui

Liu

Kuo

2015

JoVE

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Alzheimer's disease is one of a large group of neurodegenerative disorders known as tauopathies that are manifested by the neuronal deposits of hyperphosphorylated tau protein in the form of neurofibrillary tangles (NFTs). The density of NFT correlates well with cognitive impairment and other neurodegenerative symptoms, thus prompting the endeavor of developing tau aggregation-based therapeutics. Thus far, however, tau aggregation assays use recombinant or synthetic tau that is devoid of the pathology-related phosphorylation marks. Here we describe two assays using recombinant, hyperphosphorylated tau as the subject. These assays can be scaled up for high-throughput screens for compounds that can modulate the kinetics or stability of hyperphosphorylated tau aggregates. Novel therapeutics for Alzheimer's disease and other tauopathies can potentially be discovered using hyperphosphorylated tau isoforms. Video LinkThe video component of this article can be found at

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Molecular Mechanism of Tau Aggregation Induced by Anionic and Cationic Dyes

Cited by 34 publications

References 43 publications

Formation and Propagation of Tau Oligomeric Seeds

Formation and Propagation of Tau Oligomeric Seeds

SBA15–Fluconazole as a Protective Approach Against Mild Steel Corrosion: Synthesis, Characterization, and Computational Studies

<em>In Vitro</em> Aggregation Assays Using Hyperphosphorylated Tau Protein

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