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Food science & nutrition
Jan, 2020;8 (1): 620-628.

An assessment of the interaction for three flavonoids and α-amylase by surface plasmon resonance.

Pao Li, Zhao Huang, Yin She, Si Qin, Wanru Gao, Yanan Cao, Xia Liu
Author Information
  1. Pao Li: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China. ORCID
  2. Zhao Huang: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China.
  3. Yin She: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China.
  4. Si Qin: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China.
  5. Wanru Gao: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China.
  6. Yanan Cao: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China.
  7. Xia Liu: College of Food Science and Technology Hunan Provincial Key Laboratory of Food Science and Biotechnology Hunan Agricultural University Changsha China. ORCID
PMID: 31993185 DOI: 10.1002/fsn3.1349

Abstract

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.

Keywords

Chrysanthemum indicum flavonoids interaction surface plasmon resonance α‐amylase

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Journal Article

Word Cloud

Created with Highcharts 10.0.0flavonoidsα-amylaseinteractionthreeplasmonresonanceSPRstudyassay1bindinginhibitorysurfaceevaluatedCIluteolinacacetinbuddleosideSurfaceshowedequilibriumdissociationconstants9695 ± 01229240 ± 02032966 ± 008 mMpH60respectivelyFurthermoreaffinitiesinfluencedKClMgClCaClEnzymatickineticstudiesrevealedexhibitednoncompetitiveactivitysequenceluteolin > acacetin > buddleosideaccordanceresultsaffinity1-diphenyl-2-picrylhydrazylradicaldemonstratedantioxidantactivitiesinhibitedsignificantlyMeanwhilerevealshydroxylC'-4C'-5C-7playimportantroleAlsousedsensorrapidscreeninginhibitorsprovideusefulinformationapplicationfoodpharmaceuticalareaassessmentChrysanthemumindicumα‐amylase

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