Complexation of basic fibroblast growth factor with gelatin

Abstract

Polyion complexation between basic fibroblast growth factor (bFGF) and gelatin was studied by the turbidity change of mixed solution, heparin high performance liquid affinity chromatography (HPLAC), and isoelectric electrophoresis. When an aqueous solution of acidic gelatin with an isoelectric point (IEP) of 5.0 was mixed with that of bFGF, the turbidity of the mixed solution increased with time, whereas basic gelatin with and IEP of 9.0 did not cause any solution turbidity. A maximum turbidity of the mixed bFGF and acidic gelatin solution was observed around a bFGF/gelatin molar ratio of 1.0, irrespective of the gelatin concentration and solution temperature. The solution turbidity decreased with an increase in the ionic strength of the mixed solution. Complexation of bFGF with acidic gelatin was slower than that with poly(acrylic acid) probably because of the lower density of gelatin negative charge than that of poly(acrylic acid). HPLAC study revealed that complexation of bFGF with the acidic gelatin reduced the affinity of bFGF for heparin, in contrast to the basic gelatin, although the extent became smaller with the increasing ionic strength of the solution. An electrophoretic experiment showed that the IEP of bFGF shifted to a lower value after its gelatin complexation. These findings indicate that an electrostatic interaction is the main driving force for the complexation between acidic gelatin and basic bFGF.

Reconstruction of abdominal wall defects using small intestinal submucosa coated with gelatin hydrogel incorporating basic fibroblast growth factor

“…Similar to previous study 11 , the gelatin hydrogel tended to release bFGF in a burst manner at beginning 10 , that is because the impregnation condition of bFGF (e.g. at 4°C for 12h) into the acidic gelatin hydrogel is not sufficient enough to achieve 100% ionic complexation 23 .…”

“…It is reported that bFGF molecules was found to be ionically complexed with the acidic gelatin 11 , so that bFGF could be released by hydrogel degradation. In the present study, the release kinetics of bFGF was determined in temperature-controlled (37ºC) conditions.…”

“…The acidic gelatin hydrogel could ionically immobilize in bFGF, and in vivo release of bFGF is mainly governed by hydrogel biodegradation 11 . That is, the growth factor release in vivo could be controlled by biodegradation of gelatin hydrogel itself.…”

Collagen-Gelatin Scaffold Impregnated with bFGF Accelerates Palatal Wound Healing of Palatal Mucosa in Dogs

“…It was found that the remaining percentage of initially impregnated bFGF into CGS was 60% 1 wk after implantation and 30% 10 d after surgery [17]. The poly-ion complexation of acidic gelatin with bFGF prolongs its bioactivity and the collagen-gelatin matrix can enable the slow release of bFGF for up to 10 d, according to gelatin degradation [21][22][23][24]. 7. Comparison of the thickness of submucosal tissue at 1 and 2 wk after implantation.…”

Cell behavior on microparticles with different surface morphology

“…Interesting, since microparticles can be used as protein vehicles, microparticles could be used to deliver specific growth factors to enhance cell survival and differentiation [28][29][30]. Further studies of microparticles with growth factor incorporation and in vivo studies of these cell-seeded microparticles are in progress.…”