In vitro investigation of the effect of mesalazine on amyloid fibril formation of hen egg-white lysozyme and defibrillation lysozyme fibrils.

In certain conditions (such as fever and stress) mutated lysozyme enzyme deposits in different tissues and organs in the form of amyloid fibrils (plaques). These aggregates lead to tissue destruction and the pathogenesis of a disease. In this study, we investigated the in vitro effects of mesalazine drug on both preventions of lysozyme aggregation and the removal of lysozyme fibrils. With this regard, hen egg-white lysozyme (HEWL) was incubated in the absence and presence of mesalazine in high temperature and acidic pH conditions. The influence of mesalazine was surveyed by Congo red (CR) absorbance, Circular dichroism spectroscopy (CD), Thioflavin T (ThT) fluorescence assay, 1-anilinonaphthalene-8-sulfonic acid (ANS) fluorescence test, and Field-emission scanning electron microscopy (FE-SEM). Our results demonstrate that mesalazine, in all concentrations, especially in 1:1 and higher drug to protein ratios, has a strong inhibitory effect on protein fibrillation. Additionally, mesalazine does not show an acceptable impact on the reversibility of HEWL fibril in any of the related concentrations. Based on the obtained results, we conclude that mesalazine can be used as a drug for the prevention of amyloid-fibrils formation in hereditary lysozyme amyloidosis and other systemic non-neuropathic hereditary amyloidosis.