Interaction Properties of Caffeoylquinic Acid Derivatives from Ilex kudingcha C. J. Tseng with α-Amylase

doi:10.7506/spkx1002-6630-201613002

Abstract

Abstract:

The inhibitory effects of six caffeoylquinic acid (CQA) derivatives (3-CQA, 4-CQA, 5-CQA, 3,4-diCQA,
3,5-diCQA and 4,5-diCQA) against α-amylase were studied comparatively by inhibitory activity assay. Furthermore, the
potential interaction mechanisms between CQA derivative and α-amylase were investigated by fluorescence quenching and
circular dichroism (CD) spectroscopy. The binding parameters were calculated according to modified Stern-Volmer equation,
and the thermodynamic parameters were determined by the van’t Hoff equation. The results showed that all CQA derivatives
exhibited inhibitory effects on α-amylase and the half inhibitory concentrations (IC50) were 1.54, 1.05, 1.28, 0.96, 0.33 and
0.64 mg/mL, respectively. CQA derivatives interacted with α-amylase, forming stable complexes and leading to fluorescence
quenching. Thermodynamic analysis indicated that the interaction process was spontaneous, and hydrophobic force might
be primarily responsible for the interaction. In addition, the CD spectra suggested that the binding of CQA derivatives to the
enzyme induced the change of protein structure, thus destabilizing the enzyme and reducing its activity.

Key words: α-amylase, caffeoylquinic acid, fluorescence spectroscopy, circular dichroism spectrum, interaction

CLC Number:

XU Donglan, WANG Qingchuan, ZENG Xiaoxiong, SUN Yi. Interaction Properties of Caffeoylquinic Acid Derivatives from Ilex kudingcha C. J. Tseng with α-Amylase[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201613002.

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