Fungal lipase dependent processes are important virulence attributes. We explore Aspergillus niger lipase as a direct target of eugenol through spectroscopic techniques and compare results to Bovine Serum Albumin and lysozyme to comment on selectivity of eugenol towards lipase. Eugenol IC50 of lipase was 150 μg/ml. UV-vis spectroscopy shows formation of lipase-eugenol, Bovine Serum Albumin-eugenol and lysozyme-eugenol complex at concentrations well below IC50. Eugenol binding caused blue shift with Bovine Serum Albumin and lysozyme suggestive of compaction, and red shift with lipase. Negative ellipticity decreased with lipase but increased with Bovine Serum Albumin-eugenol and lysozyme-eugenol complexes suggesting loss of helical structure for lipase and compaction for Bovine Serum Albumin and lysozyme. Binding of eugenol to lipase was strong (Ka= 4.7 x 106 M-1) as compared to Bovine Serum Albumin and lysozyme. Number of eugenol binding sites on lipase is found to be 2 as compared to 1.37 (Bovine Serum Albumin) and 0.32 (lysozyme). Docking results also suggest strong binding of eugenol with lipase followed by Bovine Serum Albumin and lysozyme. To conclude, eugenol is found to be good inhibitor and disruptor of secondary and tertiary structure of lipase, whereas its binding to Bovine Serum Albumin and lysozyme is found to be weak and less disruptive of structures suggesting selectivity of eugenol towards lipase.
Keywords: Eugenol, Aspergillus niger Lipase, Bovine Serum Albumin, Lysozyme, Spectroscopy, Molecular docking
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