Investigation of the interaction of a polyamine-modified flavonoid with bovine serum albumin (BSA) by spectroscopic methods and molecular simulation

Aflatoxin B1 Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

“…While comparing the 3D fluorescence emission spectra of BSA in the presence and absence of AFB 1 , it may be noted that the fluorescence intensities of both peaks are quenched, anticipating the alteration in the microenvironment around fluorophores present in BSA after the addition of AFB 1 . 41 This result confirms conformational changes in proteins and corroborates our UV absorbance spectroscopic and fluorescence spectroscopic findings. Our findings are consistent with the previous studies on the interaction of small molecules with BSA.…”

Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties

“…This result indicates that the addition of HF changed the secondary structure of SPI. Previous studies have shown that decreasing the α-helix of protein and increasing the β-turn improves the stability of protein [20] . A study by Zou et al [21] found that ultrasound could reduce the α-helix and random coil of protein and increase the β-sheet and β-turn.…”

Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes

“…After binding with EGCG, the content of α-helix and random coil both decreased, the β-turn decreased slightly, and the β-sheet increased. These results suggest that some of the α-helix structure may have changed to β-sheet structure or may have become more disordered [ 35 ]. This effect may be because EGCG bound to the hydrophobic amino acid regions in the α-helix structure, thereby altering the spatial conformation of the pea protein molecules [ 36 ].…”