Cyanidin 3-rutinoside defibrillated bovine serum albumin under the glycation-promoting conditions: A study with multispectral, microstructural, and computational analysis

Findings small molecules with protein disaggregation effects are lately needed. For the first time, we studied the in vitro-antifibrillogenic effects of cyanidin 3-rutinoside (C3R), purified from mulberry fruits, on bovine serum albumin (BSA) under aggregation-promoting conditions, using multispectral, microstructure, and molecular docking approaches. Results showed that C3R dose-dependently inhibited BSA-aggregations under the glycation conditions through separating the size peak, influencing Trp-intensity and hydrophobicity, affecting cross-β-sheet conformations, and microstructural declining the aggregates of glycated-BSA. Throughout the underlying mechanism behind the disaggregation effects, C3R altered the secondary structure, SDS-PAGE-bands, and XRD-peaks of glycated-BSA aggregates, as well as interacted with some of lysyl and arginine (Lys114, Lys431, Arg427, and Arg185) glycation sites of BSA. Overall, these results unleash that monomeric anthocyanins restrict BSA-aggregations under the glycation conditions which can assist in the design of reasonable therapeutics and functional foods. •The defibrillation effects of C3R on glycated-BSA were studied.•C3R dose-dependently disaggregated BSA under the glycation conditions.•C3R altered the secondary structures, particles size, and spectra of glycated-BSA aggregates.•C3R interacted with some of the lysyl and arginine glycation sites of BSA.