Carl-Magnus Svahn

TL;DR: A simple assay based on a genetically engineered soluble form of murine FGF receptor 1 tagged with placental alkaline phosphatase showed that FGF-receptor binding has an absolute requirement for heparin and facilitated FGF dimerization, a property that may be important for receptor activation.

TL;DR: A framework for the molecular design of compounds capable of modulating FGF activity is established and several binding sites on FGF are revealed and constrain possible mechanisms by which heparin/HS can activate the FGF receptor.

TL;DR: The methyl glycoside of a tetrasaccharide isolated from heparin was glycosidated with a protected galactose derivative and a disaccharides block of glucuronic acid and Galactose to give tri- and tetra-saccharide derivatives, respectively to give the target compounds.

TL;DR: In this article, the tri-and tetrasaccharides present in the linkage region of heparin were synthesized together with their phosphate containing analogues, methyl O-(β-D-galactopyranosyl)-(l→3)-O-(βD-Galactophyrano-syl)-( l→4)-β-d-xylopyraniumide 2-(disodium phosphate) sodium salt, which are glycosides of the structure found in the linker of the heparan sulphate.

TL;DR: A series of disaccharides, α-l-IdoA-(l → 4)-α-d-GlcNAc-l→OMe, and two trisaccharide, β-dglcA-(1 y4)-αd-glcNac-(1 →4)-β-dGlcA-l →OMe were synthesized and tested for competitive binding to basic fibroblast growth factor in an assay using 125I labelled heparin this paper.