Mitigating the fibril formation of lysozyme using carvacrol

The misfolding of soluble protein into amyloid fibrils or oligomers leads to the disrupture of the cell membrane, cell death and various diseases related to amyloid. Therefore, inhibition of protein fibrillation is a critical and promising method for the prevention and treatment of these diseases. In the present study, the effect of carvacrol which is an important phenolic compound found in thyme plant on the formation of hen egg white lysozyme (HEWL) fibrils and also the effect of this extract on the removal of preformed fibrils was investigated. For this purpose, ۲ mg/ml HEWL in pH ۲, was incubated for ۱۴ days at ۵۷ ̊C in the presence and absence of carvacrol. The effect of the carvacrol was investigated 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 the most effective inhibition was observed in the concentration of ۰.۱۲ mg/ml of carvacrol. This compound also showed to be disaggregating of preformed fibrils Hence, carvacrol could be a potential treatment for protein misfolding and deposition diseases

Keywords:

Amyloid , Carvacrol , Lysozyme , Protein aggregation , Polyphenol