The effect of static magnetic field on inducing the binging of bovine serum albumin and cyanidin-3-O-glucoside

Serum albumin can bind with a diverse range of small molecules. It could therefore serve a protective or carrier function, and effectively address the issue of anthocyanins' susceptibility to decomposition. The anisotropic effect of the magnetic field (MF) can influence their interaction, thereby playing a distinct role in molecular bonding. In this study, bovine serum albumin (BSA) and cyanidin-3-O-glucoside (C3G) were used as raw materials. The mechanism underlying the formation of BSA-C3G complexes induced by static magnetic field (SMF) was investigated through analyses of secondary structure, functional groups, dipole moment, crystal cell dimensions, and microstructural characteristics. BSA and C3G were treated with 50, 100, 150, and 200 mT, respectively. As the magnetic intensity increased, the secondary structure of the complex changed, the α-spiral content, β-corner content, and irregular curl content decreased, while, the β-folding content increased. The average grain size of the BSA-C3G composite was observed to decrease. Furthermore, alterations in the crystal cell dimensions of the BSA-C3G complex were noted, accompanied by a tendency for the microstructure to become more flattened. This study offers valuable insights into the influence of SMF on the assembly behavior and structural characteristics of proteins and anthocyanins.