Different molecular sizes and chain conformations of water-soluble yeast β-glucan fractions and their interactions with receptor Dectin-1

被引:19
|
作者
Zheng, Zhaomin [1 ,2 ]
Huang, Qilin [1 ]
Kang, Yu [3 ]
Liu, Yonggang [3 ]
Luo, Wei [4 ]
机构
[1] Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China
[2] Hubei Univ Econ, Dept Cuisine & Nutr, Wuhan 430205, Peoples R China
[3] Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Polymer Phys & Chem, Changchun 130022, Peoples R China
[4] Changsha Univ Sci & Technol, Sch Chem & Food Engn, Changsha 410114, Peoples R China
基金
中国国家自然科学基金;
关键词
Water-soluble yeast beta-glucan; Molecular size; Chain conformation; Receptor Dectin-1; Interaction; ANTITUMOR-ACTIVITY; LIGHT-SCATTERING; SERUM-ALBUMIN; POLYSACCHARIDE; WEIGHT; FLUORESCENCE; BINDING; LIGAND; COMPLEXES; LENTINAN;
D O I
10.1016/j.carbpol.2021.118568
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Although beta-glucan could bind to Dectin-1 to exert bioactivity, the influence of molecular size and chain conformation of beta-glucan on its interaction with Dectin-1 is still unclear. This work investigated the molecular sizes and chain conformations of five water-soluble yeast beta-glucan (WYG1-5) fractions as well as their interactions with Dectin-1 by fluorescence spectroscopy and microscale thermophoresis. Results revealed a spherical conformation for higher molecular weight WYG and a stiff chain conformation for smaller molecular weight WYG. The WYG and Dectin-1 interactions were in the order of WYG-2 > WYG-1 > WYG-3 > WYG-4 > WYG-5. The spherical WYG-2 exhibited the largest binding constant of 7.91 x 10(5) M-1 and the lowest dissociation constant of 22.1 nM to Dectin-1. Additionally, the underlying interaction mechanism showed that it may be easier for spherical WYG with longer side chains to interact with receptor Dectin-1.
引用
收藏
页数:13
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