ArticleACS omega2025
Coomassie Brilliant Blue Induces Coiled-Coil Aggregation in Lysozyme at pH 7.4 by Hydrophobic and Electrostatic Forces.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Physiological Adaptations ofPlants (Basel, Switzerland) · 2025Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several neurodegenerative diseases are associated with the deposition of amyloid fibrils. Although these diseases are irreversible, knowing the aggregation mechanism is useful in developing drugs that can arrest or decrease the aggregation rate. In this study, we are interested in investigating the effect of Coomassie brilliant blue (CBB G-250) on the aggregation of hen egg white lysozyme (HEWL) at pH 7.4. Various biophysical techniques have been used, such as turbidity, Rayleigh light scattering (RLS) kinetics, far-UV circular dichroism (CD), field emission scanning electron microscopy (FESEM), and transmission electron microscopy (TEM) imaging. The turbidity data indicated that CBB (≥0.1 mM) induces aggregation in HEWL at pH 7.4. The aggregation kinetics caused by CBB are quick without a lag phase and are dependent on the CBB concentration. The far-UV CD data revealed that the CBB-induced aggregated samples had lost their CD signals without exhibiting a shift in the spectrum position. Sodium chloride and ammonium sulfate show little effect on the CBB-induced aggregates, but alcohol such as methanol, ethanol, and 2-propanol could reverse the aggregation. Overall, this study aims to better understand the mechanism underlying CBB-induced aggregation and keep in mind that CBB employed in laboratories can alter the protein structure. We report the aggregation of a natural protein due to coiled-coil formation induced by a dye at physiological pH and temperature conditions. This finding has high value because several dyes are used for diagnostic and therapeutic purposes, and coiled-coil formation is closely related to infection mechanisms and nanoparticle-based drug deliveries.
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Registered trials
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