Abstract
Eugenol has attracted considerable attention because of its potential for many pharmaceutical applications including anti-inflammatory, anti-tumorigenic and anti-oxidant properties. Here, we have investigated the effect of eugenol on amyloid formation of selected globular proteins. We find that both spontaneous and seed-induced aggregation processes of insulin and serum albumin (BSA) are significantly suppressed in the presence of eugenol. Isothermal titration calorimetric data predict a single binding site for eugenol-insulin complex confirming the affinity of eugenol for native soluble insulin species. We also find that eugenol suppresses amyloid-induced hemolysis. Our findings reveal the inherent ability of eugenol to stabilize native proteins and to delay the conversion of protein species of native conformation into β-sheet assembled mature fibrils, which seems to be crucial for its inhibitory effect.
Highlights
Effect of eugenol on amyloid formation of proteins. Amyloid formation of both insulin and serum albumin was initiated by incubating the protein monomer samples in phosphate buffer saline (PBS) at an elevated temperature close to their Tm values[25] and the aggregation kinetics was monitored by measuring Thioflavin T readings of the samples at different time points
We further have looked at Atomic force microscopy (AFM) images of mature insulin fibrils (Fig. 2a) obtained from the inhibited aggregation reactions and the results showed typical amyloid morphology as seen for insulin[28]
Current study clearly indicates that eugenol has the ability to inhibit or to interfere with the amyloid aggregation of insulin and serum albumin
Summary
As evident from the ThT signals (both for insulin and BSA), was observed to be substantially suppressed in the presence of eugenol (Fig. 1a,d). We examined the effect of 2-methoxyphenol on the aggregation process of insulin and the obtained data (Supplementary Figure S12) did not show such strong inhibition effect like eugenol.
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