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Catechol derivatives interact with bovine serum albumin: Correlation of non-covalent interactions and antioxidant activity

文献类型： 外文期刊

作者： Weng, Longmei 1 ; Li, Lin 1 ; Yang, Haitao 4 ; Ji, Lili 1 ; Wu, Ming 1 ; Wu, Yi 1 ; Chen, Zhiyi 2 ; Zhang, Xia 1 ; Li, Bing 1 ;

作者机构： 1.South China Univ Technol, Engn Res Ctr Starch & Plant Prot Deep Proc, Guangdong Prov Key Lab Green Proc Nat Prod & Prod, Sch Food Sci & Engn,Minist Educ, Guangzhou 510640, Peoples R China

2.Guangdong Acad Agr Sci, Minist Agr & Rural Affairs, Sericultural & Agrifood Res Inst, Guangdong Key Lab Agr Prod Proc,Key Lab Funct Food, Guangzhou 510610, Peoples R China

3.Dongguan Univ Technol, Sch Chem Engn & Energy Technol, Coll Rd 1, Dongguan 523808, Peoples R China

4.Fujian Med Univ, Fujian Prov Hosp, Fuzhou 350013, Peoples R China

关键词： Catechol; 1-monocaffeoyl glycerol; BSA; Multi-spectroscopic analysis; Multifunctional wavefunction; Antioxidant property

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2023 年 244 卷

页码：

收录情况： SCI

摘要： The interactions of catechol derivatives with model transportation protein-bovine serum albumin (BSA) were deciphered by the multispectral techniques, molecular docking and multifunctional wavefunction (Multiwfn). The representative catechol derivatives caffeic acid (CA) and 1-monocaffeoyl glycerol (1-MCG) with an (E)-but-2enoic acid and a 2,3-dihydroxypropyl(E)-but-2-enoate side chain, respectively, were chosen in present study. The interaction results revealed the extra non-polar interactions and abundant binding sites facilitate the easier and stronger binding of 1-MCG-BSA. The & alpha;-helix content of BSA decreased and the hydrophilicity around Tyr and Trp changed due to the different interaction between catechol and BSA. The H2O2-damaged RAW 264.7, HaCat and SH-SY5Y were applied to investigate the anti-ROS properties of the catechol-BSA complexes. The results illuminated that the 2,3-dihydroxypropyl(E)-but-2-enoate side chain of 1-MCG facilitated the preferable biocompatibility and antioxidant property of its binding complex. These results revealed that the interaction of catecholBSA binding complexes could influence their biocompatibility and antioxidant properties.

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