Interaction mechanism of benzophenone-type UV filters on bovine serum albumin: Insights from structure-affinity relationship

Abstract

Benzophenone (BP)-type UV filters can cause structural changes of carrier protein in plasma. The binding process of five BP-type UV filters with bovine serum albumin (BSA) was investigated by multiple characterization methods, along with their structure-affinity relationship involving the structure of the five BP-type UV filters and their binding affinity for BSA. The BP-type UV filters investigated bound to BSA spontaneously, and altered conformation of BSA. The binding constants and number of binding sites between BP-type UV filters and BSA were 10³–10⁶ M⁻¹ and 0.82–1.26, respectively. These BP-type UV filters and BSA interacted with the same binding forces and went through the similar binding process, suggesting that the benzophenone skeleton structure was primarily responsible for the BP-type UV filters and BSA binding, and changes in the structure of the BSA. The BP-type UV filters with hydroxyl substituent (BP-1 and BP-9) and non-polar molecules (BP-6) had a high affinity for binding BSA and had a greater impact on BSA conformation.

Keywords:

• Benzophenone-UV filters
• bovine serum albumin
• structure-affinity relationship

Data availability statement

The authors confirm that the original data supporting the findings of this study are available within the article or its supplementary materials.

Additional information

Funding

This work was supported by the Natural Science Foundation of Liaoning Province (No. 2022-MS-100).