Protective effects of three structurally similar polyphenolic compounds against oxidative damage and their binding properties to human serum albumin

Brazilin (Bra), hematoxylin (Hto) and hematein (Hte) are structurally similar polyphenols having rich biological activities, but their antioxidant ability has not been well studied. Here, their protective ability against human serum albumin (HSA) oxidative degradation were investigated using 2,2'-Azobis (2-methylpropionamidine) dihydrochloride (AAPH), NaClO and Fenton like reactions methods. The results indicated that polyphenols inhibited the oxidative injuries of HSA in the order: Hto > Bra > Hte. Additionally, the biological effects of polyphenols were mostly influenced by their binding to protein. Therefore, the structure-affinity relationships of polyphenols binding to HSA were also explored. Fluorescence experiments indicated that polyphenols bound to HSA through static quenching mechanism. Furthermore, some conformational changes of HSA could be observed in the presence of polyphenols. Altogether, molecular structure of polyphenols played a significant role in their protective effect against HSA oxidative damage and binding ability, which provided fundamental insights into their application as health care foods.

Automated summary

Brazilin, hematoxylin, and hematein are polyphenols with similar structures and rich biological activities, and they have protective effects against oxidative degradation of human serum albumin. The biological effects of these polyphenols are mainly influenced by their binding to protein, and fluorescence experiments indicate that they bind to protein through a static quenching mechanism, causing some conformational changes. These findings provide insights into the role of molecular structure in the protective effects and binding abilities of polyphenols against protein oxidative damage.