Glutaraldehyde in collagen gel formation

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Abstract
The effect of glutaraldehyde (GTA) on the course of collagen gel formation was studied by measuring the absorbance against time. It was found that the t1/2 of fibril formation decreased with the addition of GTA and reached a minimum at a concentration of 6μl of GTA per g of collagen. For GTA concentrations, [GTA], above this value, t1/2 increased again and fibril formation was inhibited at concentrations of about 50-60 μl of GTA per g of collagen. Thermal analysis showed that the denaturation temperature was the highest for the gels formed with [GTA] of 6 μl/g, the transition peak also being the sharpest. At this [GTA], the compressive rigidity of the gels was also the highest. For low [GTA], above and below the optimum value, the fibrils formed had the normal collagen periodicity when observed in the electron microscope. This study shows that collagen gels which find applications as biomaterials can be effectively crosslinked at the gelation stage itself by the addition of low concentrations of GTA.