Biotinylated basic fibroblast growth factor is biologically active

Basic fibroblast growth factor (bFGF) was modified by biotinylation via amino group substitution, using biotin-N-hydroxysuccinimide ester at molar reaction ratios of 20, 200, and 2000 per bFGF molecule (respectively named bio-bFGF.20, bio-bFGF.200, and bio-bFGF.2000). The biotinylated bFGF derivatives, bio-bFGF.20 and bio-bFGF.200, conserved the same affinity for heparin as native bFGF, in contrast to bio-FGF.2000 which lost this property. Bio-bFGF.20 and bio-bFGF.200 were as effective as native bFGF in their capacity to compete with 125I-bFGF for binding to bFGF receptor on bovine brain membranes. The biological activity of these bFGF derivatives was tested on CCL39 cells; bio-bFGF.20 and bio-bFGF.200 were as able as native bFGF to promote growth of CCL39.