Chain conformation of an acidic polysaccharide from green tea and related mechanism of α-amylase inhibitory activity

被引：35
作者：
Yin, Lin [1 ]
Fu, Shanshan [1 ]
Wu, Roujun [1 ]
Wei, Shuyue [1 ]
Yi, Juzhen [1 ,3 ]
Zhang, Li-Ming [2 ,3 ]
Yang, Liqun [1 ,3 ]
机构：
[1] Sun Yat Sen Univ, Sch Chem, Dept Polymer & Mat Sci, Guangzhou 510275, Peoples R China
[2] Sun Yat Sen Univ, Sch Mat Sci & Engn, Guangzhou 510275, Peoples R China
[3] Sun Yat Sen Univ, Key Lab Polymer Composite & Funct Mat, Guangdong Prov Key Lab High Performance Polymer B, Minist Educ, Guangzhou 510275, Peoples R China
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2020年 / 164卷
关键词：
Acidic tea polysaccharide; Chain conformation; alpha-Amylase; PU-ERH TEA; CAMELLIA-SINENSIS; IN-VITRO; MOLECULAR CHARACTERIZATION; ANTIOXIDANT; BIOACTIVITY; HYPERGLYCEMIA; POLYMERS; PROPERTY; CALCIUM;
D O I：
10.1016/j.ijbiomac.2020.07.125
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
An acidic tea polysaccharide (TPSA) isolated from green tea was fractionated using a precipitation-fractionation method into seven fractions with different molecular weights. TPSA was characterized as a hyperbranched polysaccharide with a globular homogeneous conformation by analysis of solution parameters of each fraction using static light scattering and viscosity analyses. Observation by transmission electron microscopy confirmed that TPSA occurred as globular homogeneous particles with size in the range of 20-40 nm. To simulate the branched chain segments of TPSA, four model molecules were designed based on chemical structure of TPSA. Molecular docking analysis indicated that the branched chain segments of TPSA similar to the TPSA-4 model molecule showed preferential binding to alpha-amylase to form the TPSA/alpha-amylase complex through hydrogen bonding interactions. Circular dichroism spectroscopy showed that the structure of alpha-amylase was not significantly affected by TPSA. The mechanism of alpha-amylase inhibitory activity of TPSA was simulated by molecular docking analysis. The branched chain segments of TPSA similar to the TPSA-4 model molecule likely act as a potential competitor to the starch substrate to inhibit the activity of alpha-amylase. (C) 2020 Elsevier B.V. All rights reserved.
引用
收藏
页码：1124 / 1132
页数：9
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