This study evaluated the interaction of (CI) flavonoids (luteolin, acacetin, and buddleoside) with α-amylase. Surface plasmon resonance (SPR) assay showed their equilibrium dissociation constants ( ) are 1.9695 ± 0.12, 2.9240 ± 0.20, and 3.2966 ± 0.08 mM at pH 6.0, respectively. Furthermore, their binding affinities were influenced by KCl, MgCl, and CaCl. Enzymatic kinetic studies revealed that three flavonoids exhibited noncompetitive α-amylase inhibitory activity. The inhibitory sequence is luteolin > acacetin > buddleoside, which was in accordance with the results of binding affinity from SPR. 1,1-diphenyl-2-picryl hydrazyl radical assay demonstrated that antioxidant activities of three flavonoids were inhibited significantly with α-amylase. Meanwhile, the study reveals that hydroxyl on C'-4, C'-5, and C-7 of flavonoids play an important role on the interaction of three flavonoids with α-amylase. Also, SPR could be used as sensor for rapid screening inhibitors of α-amylase and provide useful information for the application of flavonoids in food and pharmaceutical area.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6977516 | PMC |
http://dx.doi.org/10.1002/fsn3.1349 | DOI Listing |
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