1. Non-covalent Complexes Between β-lactoglobulin and Baicalein: Characteristics and Binding Properties.
- Author
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Kang, Mengchen, Du, Dehong, Zhang, Suzhi, Zhang, Shuangling, Li, Zhenru, Dongye, Zixuan, Wang, Li, Qian, Yaru, Chen, Chengwang, Cheng, Xiaofang, Ren, Yuhang, and Zhao, Bingnan
- Abstract
To better obtain protein–flavonoid complexes owned more powerful functions, non-covalent complexes between β-lactoglobulin (β-LG) and baicalein/p-coumaric acid/polydatin (Bai/p-CA/PD) were investigated. The properties of these complexes were investigated using ultraviolet (UV)-visible spectra, circular dichroism (CD) spectra, Fourier-transform infrared (FTIR), etc.; the non-covalent complexes' parameters were evaluated using fluorescence spectra and molecular docking. The peaks shifted in UV, and α-helix decreased in CD, confirming the formation of the complexes. The blue shift of amide bands and -OH peaks in FTIR indicated that the hydrophobic interactions and hydrogen bonds were strengthened. Differential scanning calorimetry (DSC) indicates that β-LG-Bai had heat resistance (improved melting peak: 188.8 °C to 195.8 °C). ABTS assay showed synergistic effects of β-LG-Bai (76.7% [β-LG-Bai] > 70.6% [β-LG + Bai], 50 μmol/L). Bai had a higher quenching ability (70.81%) than p-CA (38.69%) and PD (40.95%). The affinity order was Bai > PD > p-CA, and molecular docking binding energy (-6.02 [Bai], -5.39 [p-CA], and -5.4 kcal/mol [PD]) verified the affinity relationship. The binding constants increased with increasing temperature (2.166, 4.581, and 5.741, × 10
5 L/mol, for 298, 308, and 318 K, respectively), indicating that a higher temperature promoted stabilization of β-LG-Bai, which is consistent with hydrophobic interactions in molecular docking being the driving force of the β-LG-Bai complexes. The β-LG-Bai non-covalent complexes own synergistic antioxidant effects and improved high-temperature stability characteristics, which may have promising applications in functional foods. [ABSTRACT FROM AUTHOR]- Published
- 2024
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