Biophysical Analyses for Probing Glycan-Protein Interactions

被引:4
|
作者
Nagae, Masamichi [1 ]
Yamaguchi, Yoshiki [2 ]
机构
[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Tokyo, Japan
[2] RIKEN Cluster Pioneering Res, Synthet Cellular Chem Lab, Wako, Saitama, Japan
来源
GLYCOBIOPHYSICS | 2018年 / 1104卷
关键词
Glycan microarray; Nuclear magnetic resonance; X-ray crystallography; Isothermal titration calorimetry; Surface plasmon resonance; Molecular dynamics simulation; Frontal affinity chromatography; TRANSFER DIFFERENCE NMR; CHAIN FV FRAGMENT; STRUCTURAL-ANALYSIS; SUGAR RECOGNITION; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; BINDING MODE; 3D STRUCTURE; LECTIN; SPECTROSCOPY;
D O I
10.1007/978-981-13-2158-0_7
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
Glycan-protein interactions occur at many physiological events, and the analyses are of considerable importance for understanding glycan-dependent mechanisms. Biophysical approaches including 3D structural analysis are essential for revealing glycan-protein interactions at the atomic level. The inherent diversity of glycans suits them to function as identification tags, e.g., distinguish self from the nonself components of pathogens. However, the complexity of glycans and poor affinities for interaction partners limit the usefulness of conventional analyses. To cope with such troublesome glycans, a logical sequence of biophysical analyses need to be developed. In this chapter, we introduce a workflow of glycan-protein interaction analysis consisting of six steps: preparation of lectin and glycan, screening of glycan ligand, determination of binding epitope, quantitative interaction analysis, 3D structural analysis, and molecular dynamics simulation. Our increasing knowledge and understanding of lectin-glycan interactions will hopefully lead to the design of glyco-based medicines and vaccines.
引用
收藏
页码:119 / 147
页数:29
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