Angele Peter, Abke Jochen, Kujat Richard, Faltermeier Hubert, Schumann Detlef, Nerlich Michael, Kinner Bernd, Englert Carsten, Ruszczak Zbigniew, Mehrl Robert, Mueller Rainer
Department of Trauma Surgery, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, Regensburg 93051, Germany.
Biomaterials. 2004 Jun;25(14):2831-41. doi: 10.1016/j.biomaterials.2003.09.066.
Collagen-based scaffolds are appealing products for the repair of cartilage defects using tissue engineering strategies. The present study investigated the species-related differences of collagen scaffolds with and without 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS)-crosslinking. Resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temperature, ultrastructural matrix morphology, crosslinking density and stress-strain characteristics were determined to evaluate the physico-chemical properties of equine- and bovine-collagen-based scaffolds. Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p=0.0001), crosslinking (p=0.0001) and time (p=0.0001) on degradation of the collagen samples by collagenase treatment. Crosslinked equine collagen samples showed a significantly reduced swelling ratio compared to bovine collagen samples (p< 0.0001). The amino acid composition of equine collagen revealed a higher amount of hydroxylysine and lysine. Shrinkage temperatures of non-crosslinked samples showed a significant difference between equine (60 degrees C) and bovine collagen (57 degrees C). Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p=0.0001), crosslinking (p=0.0001) and matrix condition (p=0.0001) on rupture strength measured by stress-strain analysis. The ultrastructure, the crosslinking density and the strain at rupture between collagen matrices of both species showed no significant differences. For tissue engineering purposes, the higher enzymatic stability, the higher form stability, as well as the lower risk of transmissible disease make the case for considering equine-based collagen. This study also indicates that results obtained for scaffolds based on a certain collagen species may not be transferable to scaffolds based on another, because of the differing physico-chemical properties.
基于胶原蛋白的支架是利用组织工程策略修复软骨缺损的有吸引力的产品。本研究调查了经1-乙基-3-(3-二甲基氨基丙基)碳二亚胺(EDC)/N-羟基琥珀酰亚胺(NHS)交联和未交联的胶原蛋白支架的物种相关差异。测定了抗胶原酶消化能力、膨胀率、氨基酸序列、收缩温度、超微结构基质形态、交联密度和应力-应变特性，以评估马和牛胶原蛋白基支架的物理化学性质。三因素方差分析显示，胶原类型(p=0.0001)、交联(p=0.0001)和时间(p=0.0001)对胶原酶处理的胶原样品降解有极显著影响。与牛胶原蛋白样品相比，交联的马胶原蛋白样品的膨胀率显著降低(p<0.0001)。马胶原蛋白的氨基酸组成显示羟赖氨酸和赖氨酸含量较高。未交联样品的收缩温度在马胶原蛋白(60℃)和牛胶原蛋白(57℃)之间存在显著差异。三因素方差分析显示，胶原类型(p=0.0001)、交联(p=0.0001)和基质条件(p=0.0001)对应力-应变分析测得的断裂强度有极显著影响。两种物种胶原基质之间的超微结构、交联密度和断裂应变均无显著差异。出于组织工程目的，更高的酶稳定性、更高的形态稳定性以及更低的传染病传播风险使得考虑使用马源胶原蛋白成为理由。本研究还表明，由于物理化学性质不同，基于某一胶原蛋白物种的支架所获得的结果可能无法转移到基于另一物种的支架上。
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