کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1173662 | 1491387 | 2014 | 7 صفحه PDF | دانلود رایگان |
We have developed a rapid method that allows us to characterize the binding interaction of sulfobutylether-β-cyclodextrin (SBE-β-CD) with five therapeutically important phenolic acids: ferulic acid, caffeic acid, gallic acid, protocatechuic acid, and vanillic acid. The method utilizes a flow-injection chemiluminescence (FI-CL) technique that relies on the inhibition of a cyclodextrin-luminol chemiluminescence (CL) by increasing amounts of the phenolic acids (PAs). This loss of CL with increasing amounts of PAs fits the equation lg[(I0 − Is)/Is] = lgKPAs + nlg[PAs], allowing calculation of the binding constant (KPAs) and stoichiometric ratio (n). The five phenolic acids and SBE-β-CD formed complexes with a stoichiometric ratio of 1:1. The binding constants were on the order of 107 M−1. These results showed a good correlation with the scores calculated by molecular docking. Further investigation by site-directed molecular docking and linear correlation analysis revealed that PAs entered the larger cavity of SBE-β-CD and the formation constants mainly depended on the number of hydrogen bond acceptors in the PAs structures. All these results indicate that the CL-based affinity method can be used for direct determination of host–guest inclusion interactions and has great potential to become a reliable alternative for quantitatively studying host–guest binding and drug–protein interactions.
Journal: Analytical Biochemistry - Volume 460, 1 September 2014, Pages 54–60