Binding interactions of Trametes villosa and Trametes lactinea laccases with 4-nonylphenol and its intermediates: molecular docking and molecular dynamics approaches.
da Silva Santos RL, Bomfim NF, Motteran F
Summary
6.5/10Fungal enzymes called laccases from wood-decay fungi can break down 4-nonylphenol, a widespread pollutant that disrupts hormone systems in animals and plants; this suggests a potential biotechnology solution for cleaning contaminated water and soil.
Key Findings
Laccases from Trametes villosa and Trametes lactinea showed favorable binding affinity for 4-nonylphenol (4-NP) and its degradation intermediates via molecular docking analysis
4-NP is an emerging pollutant acting as an endocrine disruptor affecting reproductive toxicity in humans and wildlife, plus physiological disturbances in aquatic and terrestrial organisms
Electronic properties (global reactivity descriptors) of ligands correlated with laccase binding affinity, enabling structure-activity relationship predictions
Original Abstract
Emerging pollutants such as 4-nonylphenol (4-NP) act as endocrine disruptors and have been associated with reproductive toxicity in humans and wildlife, as well as with physiological disturbances in aquatic, terrestrial, and plant organisms. Laccases are oxidoreductases with notable biotechnological relevance and the ability to oxidize phenolic pollutants, making them attractive candidates for biodegradation strategies. This study investigated the interactions between laccases from Trametes villosa and Trametes lactinea and 4-NP and its degradation intermediates via molecular docking and molecular dynamics simulations (MDS). Ligands were geometrically optimized using the PM7 semiempirical method, and their global reactivity descriptors were computed to explore correlations between electronic properties and laccase binding affinity. Docking revealed favorable binding energies (ΔG