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...
| Published: |
Swansea University, Wales, UK
2025
|
|---|---|
| Institution: | Swansea University |
| Degree level: | Master of Research |
| Degree name: | MRes |
| Supervisor: | Wright, C. J. |
| URI: | https://cronfa.swan.ac.uk/Record/cronfa69822 |
| first_indexed |
2025-06-26T13:02:22Z |
|---|---|
| last_indexed |
2025-06-27T09:32:34Z |
| id |
cronfa69822 |
| recordtype |
RisThesis |
| fullrecord |
<?xml version="1.0"?><rfc1807><datestamp>2025-06-26T14:23:59.8718499</datestamp><bib-version>v2</bib-version><id>69822</id><entry>2025-06-26</entry><title>The assembly of novel collagens for regenerative medicine</title><swanseaauthors><author><sid>ee4e4d6d700244854e1ff76c5fc454eb</sid><firstname>SARAH</firstname><surname>MCCARTHY</surname><name>SARAH MCCARTHY</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2025-06-26</date><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.</abstract><type>E-Thesis</type><journal/><volume/><journalNumber/><paginationStart/><paginationEnd/><publisher/><placeOfPublication>Swansea University, Wales, UK</placeOfPublication><isbnPrint/><isbnElectronic/><issnPrint/><issnElectronic/><keywords>collagen, fibrillogenesis, Colorimetry, self-assembly, procollagen, nanofibers, fibrils, crosslinking, tissue engineering</keywords><publishedDay>29</publishedDay><publishedMonth>5</publishedMonth><publishedYear>2025</publishedYear><publishedDate>2025-05-29</publishedDate><doi/><url/><notes/><college>COLLEGE NANME</college><CollegeCode>COLLEGE CODE</CollegeCode><institution>Swansea University</institution><supervisor>Wright, C. J.</supervisor><degreelevel>Master of Research</degreelevel><degreename>MRes</degreename><apcterm/><funders/><projectreference/><lastEdited>2025-06-26T14:23:59.8718499</lastEdited><Created>2025-06-26T13:47:26.4989874</Created><path><level id="1">Faculty of Science and Engineering</level><level id="2">School of Engineering and Applied Sciences - Biomedical Engineering</level></path><authors><author><firstname>SARAH</firstname><surname>MCCARTHY</surname><order>1</order></author></authors><documents><document><filename>Under embargo</filename><originalFilename>Under embargo</originalFilename><uploaded>2025-06-26T14:01:24.9360533</uploaded><type>Output</type><contentLength>5109351</contentLength><contentType>application/pdf</contentType><version>E-Thesis – open access</version><cronfaStatus>true</cronfaStatus><embargoDate>2028-05-12T00:00:00.0000000</embargoDate><documentNotes>Copyright: The author, Sarah McCarthy, 2025</documentNotes><copyrightCorrect>true</copyrightCorrect><language>eng</language></document></documents><OutputDurs/></rfc1807> |
| spelling |
2025-06-26T14:23:59.8718499 v2 69822 2025-06-26 The assembly of novel collagens for regenerative medicine ee4e4d6d700244854e1ff76c5fc454eb SARAH MCCARTHY SARAH MCCARTHY true false 2025-06-26 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. E-Thesis Swansea University, Wales, UK collagen, fibrillogenesis, Colorimetry, self-assembly, procollagen, nanofibers, fibrils, crosslinking, tissue engineering 29 5 2025 2025-05-29 COLLEGE NANME COLLEGE CODE Swansea University Wright, C. J. Master of Research MRes 2025-06-26T14:23:59.8718499 2025-06-26T13:47:26.4989874 Faculty of Science and Engineering School of Engineering and Applied Sciences - Biomedical Engineering SARAH MCCARTHY 1 Under embargo Under embargo 2025-06-26T14:01:24.9360533 Output 5109351 application/pdf E-Thesis – open access true 2028-05-12T00:00:00.0000000 Copyright: The author, Sarah McCarthy, 2025 true eng |
| title |
The assembly of novel collagens for regenerative medicine |
| spellingShingle |
The assembly of novel collagens for regenerative medicine SARAH MCCARTHY |
| title_short |
The assembly of novel collagens for regenerative medicine |
| title_full |
The assembly of novel collagens for regenerative medicine |
| title_fullStr |
The assembly of novel collagens for regenerative medicine |
| title_full_unstemmed |
The assembly of novel collagens for regenerative medicine |
| title_sort |
The assembly of novel collagens for regenerative medicine |
| author_id_str_mv |
ee4e4d6d700244854e1ff76c5fc454eb |
| author_id_fullname_str_mv |
ee4e4d6d700244854e1ff76c5fc454eb_***_SARAH MCCARTHY |
| author |
SARAH MCCARTHY |
| author2 |
SARAH MCCARTHY |
| format |
E-Thesis |
| publishDate |
2025 |
| institution |
Swansea University |
| college_str |
Faculty of Science and Engineering |
| hierarchytype |
|
| hierarchy_top_id |
facultyofscienceandengineering |
| hierarchy_top_title |
Faculty of Science and Engineering |
| hierarchy_parent_id |
facultyofscienceandengineering |
| hierarchy_parent_title |
Faculty of Science and Engineering |
| department_str |
School of Engineering and Applied Sciences - Biomedical Engineering{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Engineering and Applied Sciences - Biomedical Engineering |
| document_store_str |
0 |
| active_str |
0 |
| description |
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. |
| published_date |
2025-05-29T05:29:11Z |
| _version_ |
1851097928679030784 |
| score |
11.444473 |

