Curcumin inhibits the Al(iii) and Zn(ii) induced amyloid fibrillation of β-lactoglobulin in vitro. Issue 112 (23rd November 2016)

• Record Type: Journal Article
• Authors: Pal, Sampa; Maity, Sanhita; Sardar, Subrata; Parvej, Hasan; Das, Niloy; Chakraborty, Jishnu; Chandra Halder, Umesh
• Is Part Of: RSC advances. Volume 6:Issue 112(2016)
• Page Start: 111299
• Page End: 111307
• Publication Date: 2016-11-23
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra24570f
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Accumulation of ordered protein aggregates (or amyloids) is responsible for several neurodegenerative diseases. Abstract : Accumulation of ordered protein aggregates (or amyloids) is responsible for several neurodegenerative diseases. The behaviour of amyloidal fibril formation of β-lactoglobulin (β-lg) during heat treatment depends on the environmental conditions. In this study the Al(iii ) and Zn(ii ) induced amyloid fibrillations of β-lg, in the absence and presence of curcumin, were evaluated using fluorescence, Thioflavin T, Congo red, Rayleigh scattering, dynamic light scattering analysis, FT-IR, CD spectroscopy and transmission electron microscopy. Curcumin, a natural phenolic antioxidant, is capable of binding with Al 3+, Zn 2+ and β-lg. Our experimental findings demonstrate that the metal–curcumin mixture can inhibit the transition from less structured oligomers to β-sheet rich protofibrils which act as seeding factors for further fibrillization. The Al(iii )–curcumin mixture has greater inhibition capability than the Zn(ii )–curcumin mixture of heat treated metal induced aggregation of β-lg.