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dc.contributor.authorJin, Weihua
dc.contributor.authorJiang, Di
dc.contributor.authorZhang, Wenjing
dc.contributor.authorWang, Chunyu
dc.contributor.authorXia, Ke
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.identifier.citationInteractions 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.
dc.descriptionInternational Journal of Biological Macromolecules, 160, 26–34
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractA 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.
dc.description.sponsorshipNational Institutes of Health
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleInteractions of Fibroblast Growth Factors with Sulfated Galactofucan from Saccharina japonica
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)

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