ArticleChemphyschem : a European journal of chemical physics and physical chemistry2026
Complexation of Hen Egg White Lysozyme With Bioactive Phenolic Acids: Molecular Insights Into the Binding Mechanisms and Inhibitory Effects Against Protein Aggregation.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2026. 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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Who cites it
1 citing paper in PubMed.
- Complexation of Hen Egg White Lysozyme With Bioactive Phenolic Acids: Molecular Insights Into the Binding Mechanisms and Inhibitory Effects Against Protein Aggregation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
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7 authors.
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Abstract
Protein misfolding and aggregation are central to many protein aggregation disorders, highlighting the need for effective aggregation inhibitors. This study investigated fructose-induced aggregation of hen egg-white lysozyme (HEWL) and its modulation by the phenolic acids ferulic acid (FA), caffeic acid (CA) and chlorogenic acid (CGA) at 100 and 200 μM. Circular dichroism and ThT fluorescence assays showed that fructose promoted aggregation through increased β-sheet content and fluorescence intensity, respectively, whereas all phenolic acids suppressed β-sheet formation. CA displayed the highest aggregation inhibition activity, followed by FA and CGA. FESEM imaging confirmed fructose-induced HEWL aggregation without fibril formation and demonstrated disruption of aggregates in the presence of phenolic acids. These findings were explained by other biophysical characterisation studies. Fluorescence spectroscopy indicated a static quenching mechanism for all complexes, with FA and CA displaying atypical quenching behaviour. Binding constants suggested moderate affinity, with CA (4.11 ± 0.57 × 10
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