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Interaction mechanism of benzophenone-type UV filters on bovine serum albumin: Insights from structure-affinity relationship.
Liu, Hongrui; Ma, Yanxuan; Li, Xiang; Gu, Jiali; Dong, Dianbo.
Afiliação
  • Liu H; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, PR China.
  • Ma Y; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, PR China.
  • Li X; Shenyang Photosensitive Chemical Research Institute Co. Ltd., Shenyang, PR China.
  • Gu J; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, PR China.
  • Dong D; Liaoning Academy of Environmental Sciences, Shenyang, PR China.
Article em En | MEDLINE | ID: mdl-36416057
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Benzofenonas / Soroalbumina Bovina Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Benzofenonas / Soroalbumina Bovina Idioma: En Ano de publicação: 2022 Tipo de documento: Article