Abstract
In this study, chemical chaperone like function of cyanidin-3-O-glucoside (C3G) was investigated through fluorescence spectroscopy, UV–visible spectroscopy, circular dichroism spectroscopy, confocal microscopy, scanning electron microscopy and molecular docking studies. Early and advanced glycation inhibitory effect was evaluated by fluorescence spectroscopy and agarose gel electrophoresis. Amyloids were investigated based on their propensity to bind Congo Red (CR) and Thioflavin T (ThT) by multiple microscopic approaches. Circular dichroism studies were used to analyze the changes in the secondary structure due to glycation. C3G effectively inhibited early and advanced glycation by masking like function, carbonyl scavenging and chemical chaperone activity. C3G had molecular interaction with Glu186, Arg427, Ser428, Lys431, Arg435, and Arg458 of BSA. Based on the microscopic analysis, it is evident that C3G can inhibit protein aggregation and amyloid formation. Circular dichroism studies suggested that glycation had resulted in augmented β-sheet propensity, whereas C3G had a protective effect on the helical conformation of BSA. We conclude that C3G has a chemical chaperone like function on the event of glycation mediated amyloid formation in BSA.
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