INTERACTIONS OF PUTATIVE HEPARIN-BINDING DOMAINS OF BASIC FIBROBLAST GROWTH-FACTOR AND ITS RECEPTOR, FGFR-1, WITH HEPARIN USING SYNTHETIC PEPTIDES

We have examined structure-function relationships that have been propo sed to account for the heparin-binding properties of basic fibroblast growth factor and its receptor, FGFR-1, using synthetic peptides, DNA synthesis assays and binding assays in a resonant mirror biosensor. Th e results suggest that the interaction of FGFR-1 with heparin may not be physiologically relevant and that the site of interaction of the po lysaccharide on bFGF is more complex than has been anticipated.