Temperature, pH and additives effects on the binding of Caffeic acid phenethyl ester to the native state of bovine serum albumin

The Journal of Chemical Thermodynamics(2022)

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摘要
•The quenching mechanism is static quenching.•The interaction forces are hydrogen bond and van der Waals force.•CAPE changes the secondary structure of BSA.•The interaction between CAPE and BSA are found to be affected by the change of pH, temperature and additives.
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关键词
Caffeic acid phenethyl ester (CAPE),Bovine serum albumin (BSA),Binding constant,Molecular docking
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