Novel collagen scaffolds prepared by using unnatural D-amino acids assisted EDC/NHS crosslinking
| Autor: | S. Sadulla, Asit Baran Mandal, P.K. Sehgal, Ganesan Krishnamoorthy |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Thermogravimetric analysis
Materials science Biocompatibility Cell Survival Protein Conformation Scanning electron microscope Biomedical Engineering Biophysics Succinimides Biocompatible Materials Bioengineering Biomaterials Mice chemistry.chemical_compound Succinimide Ethyldimethylaminopropyl Carbodiimide Ultimate tensile strength Polymer chemistry Cell Adhesion Animals Denaturation (biochemistry) Collagenases Amino Acids Elastic modulus Mechanical Phenomena Tissue Scaffolds Temperature Water Biomaterial Molecular Docking Simulation Cross-Linking Reagents chemistry Chemical engineering Proteolysis NIH 3T3 Cells Cattle Collagen Clostridium histolyticum |
| Zdroj: | Journal of Biomaterials Science, Polymer Edition. 24:344-364 |
| ISSN: | 1568-5624 0920-5063 |
| DOI: | 10.1080/09205063.2012.690280 |
| Popis: | 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 (Tg, 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-D-AAs 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. |
| Databáze: | OpenAIRE |
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