Cyanidin 3-rutinoside defibrillated bovine serum albumin under the glycation-promoting conditions: A study with multispectral, microstructural, and computational analysis
Ibrahim Khalifa, Remah Sobhy, Asad Nawaz, Wei Xiaoou, Zhihua Li, Xiaobo Zou
International Journal of Biological Macromolecules
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.
Circular dichroism, Secondary structure, Aggregation, Food science, Biochemistry