2014
DOI: 10.1002/bip.22486
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Collagen‐based biomaterials for wound healing

Abstract: With its wide distribution in soft and hard connective tissues, collagen is the most abundant of animal proteins. In vitro, natural collagen can be formed into highly organized, three-dimensional scaffolds that are intrinsically biocompatible, biodegradable, non-toxic upon exogenous application, and endowed with high tensile strength. These attributes make collagen the material of choice for wound healing and tissue engineering applications. In this article, we review the structure and molecular interactions o… Show more

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Cited by 837 publications
(673 citation statements)
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References 163 publications
(205 reference statements)
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“…However, in pathological processes, such as the chronic wound, fibrillar collagen is susceptible to degradation by multiple proteolytic enzymes, including MMP-1, -2, -8, -13, and -14. 22,23 Initial cleavage of Col I results in two large fragments that can then spontaneously unwind into nonhelical gelatin derivatives which are susceptible to degradation by nonspecific proteases and gelatinases. Degradation of collagen into gelatin results in loss of the cellular binding capacity and ability to sequester inflammatory mediators.…”
Section: Collagen Components In the Ecmmentioning
confidence: 99%
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“…However, in pathological processes, such as the chronic wound, fibrillar collagen is susceptible to degradation by multiple proteolytic enzymes, including MMP-1, -2, -8, -13, and -14. 22,23 Initial cleavage of Col I results in two large fragments that can then spontaneously unwind into nonhelical gelatin derivatives which are susceptible to degradation by nonspecific proteases and gelatinases. Degradation of collagen into gelatin results in loss of the cellular binding capacity and ability to sequester inflammatory mediators.…”
Section: Collagen Components In the Ecmmentioning
confidence: 99%
“…Chemical cross-linking may increase stability; however, the covalent bonds between the polymeric chains may be cytotoxic when the material is degraded. 23,25 Alternative methods to increase stability include electrostatic cross-linking with chitosan or stabilization through hydrogen bonding with sugars or polyphenols. 15,22 These methods stabilize the material structure and may increase the efficiency of chemical cross-linking without reducing the biological performance.…”
Section: Structure Modification Through Processingmentioning
confidence: 99%
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“…Advantages of using collagen as a biomaterial for tissue engineering are well documented. (17,18) Collagen is highly biocompatible and is the most abundant organic material in the body. (19) Collagen has been successfully employed in hydrogel form or as cell culture substrates with several collagen-based matrices for tissue regeneration in commercial use.…”
Section: Introductionmentioning
confidence: 99%
“…13,14 Collagen's glycine-X-Y tripeptide repeating sequence, together with the unique sequences embedded within the tripeptide repeats required for cell interaction sites, and the large overall number of amino acids, result in difficulties in generating an encoding synthetic gene due to oligonucleotide mishybridizations. 15 Furthermore, prolines in the Y position must be posttranslationally hydroxylated for sufficient thermostability of the collagen triple helix.…”
Section: Introductionmentioning
confidence: 99%