Ng Hon Wei, Zhang Yi, Naffa Rafea, Prabakar Sujay
Leather and Shoe Research Association of New Zealand, P.O. Box 8094, Palmerston North 4472, New Zealand.
Gels. 2020 Nov 27;6(4):46. doi: 10.3390/gels6040046.
Collagen-based hydrogels are investigated extensively in tissue engineering for their tunable physiochemical properties, biocompatibility and biodegradability. However, the effect of the integrity of the collagen triple helical structure on biodegradability is yet to be studied. In this study, we monitored the degradation of intact collagen (C-coll) and hydrolyzed collagen (D-coll) hydrogels in collagenase to understand their degradation process. Our results show that when peptides are present on the surface of the fibrils of D-coll hydrogels, cleavage of amide bonds occur at a much higher rate. The fibrillar structure of D-coll hydrogel results in a more pronounced breakdown of the gel network and dissolution of collagen peptides. The results from this work will improve the understanding of enzymatic degradation and the resulting bioabsorption of collagen materials used in drug delivery systems and scaffolds.
基于胶原蛋白的水凝胶因其可调节的物理化学性质、生物相容性和生物降解性而在组织工程中得到广泛研究。然而,胶原蛋白三螺旋结构的完整性对生物降解性的影响尚未得到研究。在本研究中,我们监测了完整胶原蛋白(C-coll)和水解胶原蛋白(D-coll)水凝胶在胶原酶中的降解情况,以了解它们的降解过程。我们的结果表明,当肽存在于D-coll水凝胶的原纤维表面时,酰胺键的断裂速率要高得多。D-coll水凝胶的纤维状结构导致凝胶网络更明显的分解和胶原蛋白肽的溶解。这项工作的结果将增进对酶促降解以及药物递送系统和支架中使用的胶原蛋白材料的生物吸收的理解。