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In silico studies show gyrophoric acid effectively inhibits amyloid beta peptide aggregation, highlighting its potential for Alzheimer’s therapy.
Alzheimer’s disease (AD) is characterized by amyloid-beta (Aβ) plaque accumulation and neurodegeneration. This study identifies gyrophoric acid, a lichen-derived phenolic metabolite, as a dual-action Aβ42 inhibitor preventing aggregation and disassembling of mature Aβ42 fibrils. Integrated the in silico studies revealed that gyrophoric acid was a strong thermodynamic stabilizer of Aβ42 (MM-GBSA: -27.3 kcal/mol) via entropically driven hydrophobic interactions and disruption of aggregation-prone conformations (100-ns MD simulations). Through biochemical analysis of the fluorescent dye Thioflavin T (ThT), gyrophoric acid induced the rapid Aβ42 fibril disassembly within 5 hours, with time-lapse confocal microscopy quantitatively confirming the near-complete dissolution of large aggregates by 24 hours. ADMET profiling revealed favourable pharmacokinetics (moderate oral absorption: 48.5–57.3%; low toxicity) and Lipinski’s rule compliance. These results establish gyrophoric acid as a promising natural bioactive compound leading for anti-AD therapeutics, with a unique hydrophobic-stabilization mechanism.
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Yang et al. (2025) studied this question.
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