Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis

July 28, 2017

Title

Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis

Author

Kriti Dubey, Bibin G. Anand, Dolat Singh Shekhawat, Karunakar Kar

Year

2017

Journal

Scientific Reports

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.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Aggregation, Biochemistry