Interactions of Fibroblast Growth Factors with Sulfated Galactofucan from Saccharina japonica

Authors
Jin, Weihua
Jiang, Di
Zhang, Wenjing
Wang, Chunyu
Xia, Ke
Zhang, Fuming
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2020-10-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Interactions of Fibroblast Growth Factors with Sulfated Galactofucan from Saccharina japonica, W. Jin, D. Jiang, W. Zhang, C. Wang, K. Xia, F. Zhang, R. J. Linhardt, International Journal of Biological Macromolecules, 160, 26–34, 2020.
Abstract
A total 68 types of marine algae oligosaccharides and polysaccharides were prepared and used to study the structure-activity relationship of oligosaccharides and polysaccharides in their interactions with fibroblast growth factors (FGF) 1 and 2. Factors considered include different types of algae, extraction methods, molecular weight, sulfate content and fractions. In the case of low molecular weight polysaccharide (SJ-D) from Saccharina japonica and its fractions eluting from anion exchange column, both 1.0 M NaCl fraction (SJ-D-I) and 2.0 M NaCl fraction (SJ-D-S) had stronger binding affinity than the parent SJ-D, suggesting that sulfated galactofucans represented the major tight binding component. Nuclear magnetic resonance showed that SJ-D-I was a typical sulfated galactofucan, composed of four units: 1, 3-linked 4-sulfated α-L-fucose (Fuc); 1, 3-linked 2, 4-disulfated α-L-Fuc; 1, 6-linked 4-sulfated β-D-Gal and/or 1, 6-linked 3, 4-sulfated β-D-Gal. Modification by autohydrolysis to oligosaccharides and desulfation decreased the FGF binding affinity while oversulfation increased the affinity. The solution-based affinities of SJ-D-I to FGF1 and FGF2 were 69 nM and 3.9 nM, suggesting that SJ-D-I showed better preferentially binding to FGF1 than a natural ligand, heparin, suggesting that sulfated galactofucan might represent a good regulator of FGF1.
Description
International Journal of Biological Macromolecules, 160, 26–34
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
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Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
International Journal of Biological Macromolecules
https://harc.rpi.edu/
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