Mitigating the fibril formation of lysozyme using carvacrol

The misfolding of soluble protein into amyloid fibrils or oligomers leads to the disrupture of the cellmembrane, cell death and various diseases related to amyloid. Therefore, inhibition of proteinfibrillation is a critical and promising method for the prevention and treatment of these diseases. In thepresent study, the effect of carvacrol which is an important phenolic compound found in thyme plant onthe formation of hen egg white lysozyme (HEWL) fibrils and also the effect of this extract on theremoval of preformed fibrils was investigated. For this purpose, ۲ mg/ml HEWL in pH ۲, was incubatedfor ۱۴ days at ۵۷ ̊C in the presence and absence of carvacrol. The effect of the carvacrol wasinvestigated using a wide range of assays, including Thioflavin T (ThT) fluorescence measurement,circular dichroism (CD) spectroscopy, transmission electron microscopy (TEM) and molecular docking(MD) analysis. It was shown that HEWL fibrillation was significantly inhibited by carvacrol, and themost effective inhibition was observed in the concentration of ۰.۱۲ mg/ml of carvacrol. This compoundalso showed to be disaggregating of preformed fibrils. Hence, carvacrol could be a potential treatmentfor protein misfolding and deposition diseases.

Keywords:

Amyloid , Carvacrol , Lysozyme , Protein aggregation , Polyphenol