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Novel Biomedical Applications of Crosslinked Collagen
Collagen is one of the most useful biopolymers because of its low immunogenicity and biocompatibility. The biomedical potential of natural collagen is limited by its poor mechanical strength, thermal stability, and enzyme resistance, but exogenous chemical, physical, or biological crosslinks have be...
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Published in: | Trends in biotechnology (Regular ed.) 2019-05, Vol.37 (5), p.464-491 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Collagen is one of the most useful biopolymers because of its low immunogenicity and biocompatibility. The biomedical potential of natural collagen is limited by its poor mechanical strength, thermal stability, and enzyme resistance, but exogenous chemical, physical, or biological crosslinks have been used to modify the molecular structure of collagen to minimize degradation and enhance mechanical stability. Although crosslinked collagen-based materials have been widely used in biomedicine, there is no standard crosslinking protocol that can achieve a perfect balance between stability and functional remodeling of collagen. Understanding the role of crosslinking agents in the modification of collagen performance and their potential biomedical applications are crucial for developing novel collagen-based biopolymers for therapeutic gain.
Multiple crosslinking techniques have been developed to optimize the properties of fibrillar collagen for different biotechnological applications.
Treatments based on modulating crosslinks within the collagen matrix of damaged tissues have received excellent clinic results for treating diseases such as keratoconus.
Crosslinked collagen-based scaffolds have been extensively studied for tissue engineering to promote tissue regeneration or repair.
Nanoparticles act as crosslinking agents for collagen stabilization as well as functionalized carriers for crosslinking to collagen scaffolds for novel biomolecular applications. |
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ISSN: | 0167-7799 1879-3096 |
DOI: | 10.1016/j.tibtech.2018.10.007 |