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首页> 外文期刊>Journal of biomaterials science >Novel collagen scaffolds prepared by using unnatural D-amino acids assisted EDC/NHS crosslinking
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Novel collagen scaffolds prepared by using unnatural D-amino acids assisted EDC/NHS crosslinking

机译:通过使用非天然D-氨基酸辅助的EDC / NHS交联制备的新型胶原蛋白支架

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This work discusses the preparation and characterization of novel collagen scaffolds by using unnatural D-amino acids (Coll-D-AAs)-assisted 1-ethyl-3-(3-dimethylaminopropyl)- carbodiimide (EDC)/N-hydroxyl succinimide(NHS)-initiated crosslinking. The mechanical strength, hydrothermal and structural stability, resistance to biodegradation and the biocompatibility of Coll-D-AAs matrices were investigated. The results from Thermo mechanical analysis, Differential scanning calorimetric analysis and Thermo gravimetric analysis of the Coll-D-AAs matrices indicate a significant increase in the tensile strength (TS, 180 ± 3), % elongation (% E, 80 ± 9), elastic modulus (E, 170 ± 4) denaturation temperature (T_d, 108 ± 4) and a significant decrease in decomposition rate (T_g, 64 ± 6). Scanning electron microscopic and Atomic force microscopic analyses revealed a well-ordered with properly oriented and well-aligned structure of the Coll-D-AAs matrices. FT-IR results suggest that the incorporation of D-AAs favours the molecular stability of collagen matrix. The D-AAs stabilizing the collagen matrices against degradation by collagenase would have been brought about by protecting the active sites in collagen. The Coll-D-AAs matrices have good biocompatibility when compared with native collagen matrix. Molecular docking studies also indicate better understanding of bonding pattern of collagen with D-AAs. These Coll-DAAs matrices have been produced in high mechanical strength, thermally and biologically stable, and highly biocompatible forms that can be further manipulated into the functional matrix suitable in designing scaffolds for tissue engineering and regenerative medical applications.
机译:这项工作讨论了使用非天然D-氨基酸(Coll-D-AAs)辅助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)制备和表征新型胶原蛋白支架的方法)引发的交联。研究了Coll-D-AAs基质的机械强度,水热和结构稳定性,抗生物降解性以及生物相容性。 Coll-D-AAs矩阵的热机械分析,差示扫描量热分析和热重分析的结果表明,抗张强度(TS,180±3),伸长%(%E,80±9)显着增加,弹性模量(E,170±4)变性温度(T_d,108±4)和分解速率显着降低(T_g,64±6)。扫描电子显微镜和原子力显微镜分析显示了Coll-D-AAs矩阵的排列整齐,方向正确且排列合理。 FT-IR结果表明D-AA的掺入有利于胶原基质的分子稳定性。通过保护胶原蛋白中的活性位点可以实现稳定胶原蛋白矩阵抵抗胶原酶降解的D-AA。与天然胶原蛋白基质相比,Coll-D-AAs基质具有良好的生物相容性。分子对接研究还表明,人们对D-AAs与胶原蛋白的结合方式有了更好的了解。这些Coll-DAA基质以高机械强度,热和生物稳定性以及高度生物相容性形式生产,可以进一步加工成功能基质,适用于设计组织工程和再生医学应用的支架。

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