کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1220409 | 1494613 | 2016 | 8 صفحه PDF | دانلود رایگان |
• Probing a distinctive pharmacokinetic interaction between caffeic acid phenethyl ester (CAPE) and human serum albumin (HAS) in vitro.
• Binding affinity of CAPE and HAS is much stronger than that of the other propolis components.
• CAPE binds on HSA subdomain IIA through hydrogen bonds and van der Waals force.
• Binding distance of CAPE and HAS (5.7 nm) is longer than that of the other propolis components.
Caffeic acid phenethyl ester (CAPE), as one of the major bioactive components present in propolis, exhibits versatile bioactivities, especially for its potent cytotoxic effects on several cancer cell models. To understand the pharmacokinetic characteristics of CAPE, the binding interaction between CAPE and human serum albumin (HSA) was investigated in vitro using multiple spectroscopic methods and molecular docking. The results reveal that CAPE exhibits a distinctive binding interaction with HSA comparing with other propolis components. The association constant KA (L mol−1) of the binding reaches 106 order of magnitude, which is significantly stronger than the other components of propolis. Based on the theory of fluorescence resonance energy transfer, the binding distance was calculated as 5.7 nm, which is longer than that of the other components of propolis. The thermodynamic results indicate that the binding is mainly driven by hydrogen bonds and van der Waals force. The docking and drugs (warfarin and ibuprofen) competitive results show that CAPE is located in the subdomain IIA (Sudlow’s site I, FA7) of HSA, and Gln196 and Lys199 contribute to the hydrogen bonds. Circular dichroism spectra suggest an alteration of the secondary structure of HSA due to its partial unfolding in the presence of CAPE.
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Journal: Journal of Pharmaceutical and Biomedical Analysis - Volume 122, 15 April 2016, Pages 21–28