Structural analysis of synthetic heparan sulfate oligosaccharides with fibroblast growth factors and heparin-binding hemagglutinin
| Autor: | Chia-Lin Chyan, Medel Manuel L. Zulueta, Shang-Cheng Hung |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Molecular Structure Hydrogen bond Heparan sulfate Plasma protein binding Hemagglutinin 010402 general chemistry Fibroblast growth factor 01 natural sciences 0104 chemical sciences Hydrophobic effect Fibroblast Growth Factors 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship 030104 developmental biology chemistry Biochemistry Structural Biology Lectins Structure–activity relationship Heparitin Sulfate Sulfate Molecular Biology Protein Binding |
| Zdroj: | Current opinion in structural biology. 50 |
| ISSN: | 1879-033X |
| Popis: | Heparan sulfate interacts with a variety of proteins at the cell surface. These proteins are primarily attracted to the high negative charge distribution brought by sulfate, sulfamate, and carboxylate functionalities along the sugar chain. Apart from electrostatic interactions, hydrogen bonding and even hydrophobic interactions contribute to the complex formation. While additional sulfate/sulfamate groups are often tolerated as long as the main structural requirements are met, occasionally, certain extra sulfate groups may be detrimental to the binding affinity. Here, we show these binding characteristics using the binding of fibroblast growth factors and heparin-binding hemagglutinin to synthetic heparan sulfate oligosaccharides as examples. Insights into the binding characteristics of these proteins may benefit future therapeutic interventions. |
| Databáze: | OpenAIRE |
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