E-Thesis 184 views
The assembly of novel collagens for regenerative medicine / SARAH MCCARTHY
Swansea University Author: SARAH MCCARTHY
Abstract
Collagen is the primary structural protein in the extracellular matrix (ECM) and plays a pivotal role in tissue integrity, repair, and regeneration. Due to its biocompatibility and mechanical resilience, collagen has become a cornerstone in biomedical engineering, tissue scaffolding, and regenerativ...
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Swansea University, Wales, UK
2025
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| Institution: | Swansea University |
| Degree level: | Master of Research |
| Degree name: | MRes |
| Supervisor: | Wright, C. J. |
| URI: | https://cronfa.swan.ac.uk/Record/cronfa69822 |
| Abstract: |
Collagen is the primary structural protein in the extracellular matrix (ECM) and plays a pivotal role in tissue integrity, repair, and regeneration. Due to its biocompatibility and mechanical resilience, collagen has become a cornerstone in biomedical engineering, tissue scaffolding, and regenerative medicine. However, naturally derived collagen presents challenges such as batch-to-batch variability, immunogenicity, and limited mechanical stability. This study investigates the assembly, modification, and functional properties of novel engineered collagens to address these limitations and optimize their use in regenerative medicine.A multidisciplinary approach combining biochemical analysis, recombinant protein engineering, and advanced microscopy techniques was employed to characterize collagen assembly at the molecular level. Using mass spectrometry, atomic force microscopy (AFM),and rheological analysis, we examined the structural stability, cross-linking behavior, and mechanical properties of engineered collagen matrices. Additionally, in vitro cell culture studies assessed the interaction of novel collagen scaffolds with fibroblasts and mesenchymal stem cells, evaluating adhesion, proliferation, and differentiation potential.Our findings demonstrate that engineered collagens with controlled hydroxylation, optimized cross-linking, and enhanced fibril formation exhibit superior biomechanical strength, thermal stability, and cellular compatibility compared to native collagen. The results highlight their potential as next-generation biomaterials for applications in wound healing, cartilage regeneration, and tissue scaffolding. Future studies will focus on in vivo validation, large-scale production, and clinical translation to further establish engineered collagen as a viable alternative to traditional biomaterials in regenerative medicine. |
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| Keywords: |
collagen, fibrillogenesis, Colorimetry, self-assembly, procollagen, nanofibers, fibrils, crosslinking, tissue engineering |
| College: |
Faculty of Science and Engineering |