Investigation the protective ability of H. sabdariffa aqueous extract on the aggregatin of α-lactalbmin

protein aggregates generated by different reason, cause many diseases in humans and other organisms. Finding proper ways to stabilize or prevent of protein aggregation could be important. H. sabdariffa is a good source of natural antioxidants which may protect the body from damage effeccted by free radicals. This study examined the effect of aqueous extract of H. sabdariffa on the aggregation of reduced α-lactalbumin. The chaperone properties of H. sabdariffa extract on protein aggregation were determined by measuring light scattering absorption, thioflavin T binding assay, fluorescence, and circular dichroism (CD) spectroscopy. Visible absorption spectroscopy and ThT fluorescence results shows that H. sabdariffa extract prevent protein aggregation and amyloid formation in a concentration-dependent manner. According to the results of Fluorescence Spectroscopy, H. sabdariffa extract interact with hydrophobic area of protein and inhibit aggregation. CD spectroscopy results shows that DTT caused changes in secondary structure of protein and in the presence of extract, fewer changes observed. Our finding suggests the possibility of using H. sabdariffa extract as a potential agent for inhibition of protein aggregation in various disease