Journal
MOLECULAR BIOSYSTEMS
Volume 7, Issue 6, Pages 1883-1890Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1mb05008g
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Funding
- Shanghai Rising-Star Program [11QA1404700]
- Natural Science Foundation of Shanghai [10ZR1421700]
- Shanghai Municipal Education Commission [10YZ68, J50401]
- Shanghai Education Development Foundation [09CG46]
- Shanghai Normal University [SK201006]
- National Transgenic Organism New Variety Culture Key Project [2009ZX08012-002B]
- National Natural Science Fund [30900110]
- Ministry of Science and Technology of China [NC2010AE0075, NC2010AE0372]
- Shanghai Science and Technology Committee [10JC1412000, 09QH1401900, 08391911800]
- Fujian Science and Technology Committee [2008NZ0001-4]
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The relationship between the structural properties of natural polyphenols and their affinities for alpha-amylase were investigated by fluorescence titration analysis. The binding process with alpha-amylase was strongly influenced by the structural differences of the compounds under study. For instance, the methylation of the hydroxyl group in flavonoids increased their binding affinities for alpha-amylase by 2.14 to 7.76 times. The hydroxylation on rings A, B, and C of flavonoids also significantly affected their affinities for alpha-amylase. The glycosylation of isoflavones and flavanones reduced their affinities for alpha-amylase and the glycosylation of flavones and flavonols enhanced their affinities for alpha-amylase. Hydrogenation of the C2=C3 double bond of flavonoids decreased the binding affinities. The galloylated catechins had higher binding affinities with alpha-amylase than non-galloylated catechins and the pyrogallol-type catechins had higher affinities than the catechol-type catechins. The presence of the galloyl moiety is the most decisive factor. The glycosylation of resveratrol decreased its affinity for alpha-amylase. The esterification of gallic acid significantly reduced the affinity for alpha-amylase. The binding interaction between polyphenols and alpha-amylase was mainly caused by hydrophobic forces.
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