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Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis
Date Issued
2017-02-01
Author(s)
Dubey, Kriti
Anand, Bibin G.
Shekhawat, Dolat Singh
Kar, Karunakar
DOI
10.1038/srep40744
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.