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Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum

Collagen-based hydrogels are investigated extensively in tissue engineering for their tunable physiochemical properties, biocompatibility and biodegradability. However, the effect of the integrity of the collagen triple helical structure on biodegradability is yet to be studied. In this study, we mo...

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Detalles Bibliográficos
Autores principales: Ng, Hon Wei, Zhang, Yi, Naffa, Rafea, Prabakar, Sujay
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7709630/
https://www.ncbi.nlm.nih.gov/pubmed/33260949
http://dx.doi.org/10.3390/gels6040046
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author Ng, Hon Wei
Zhang, Yi
Naffa, Rafea
Prabakar, Sujay
author_facet Ng, Hon Wei
Zhang, Yi
Naffa, Rafea
Prabakar, Sujay
author_sort Ng, Hon Wei
collection PubMed
description Collagen-based hydrogels are investigated extensively in tissue engineering for their tunable physiochemical properties, biocompatibility and biodegradability. However, the effect of the integrity of the collagen triple helical structure on biodegradability is yet to be studied. In this study, we monitored the degradation of intact collagen (C-coll) and hydrolyzed collagen (D-coll) hydrogels in collagenase Clostridium histolyticum to understand their degradation process. Our results show that when peptides are present on the surface of the fibrils of D-coll hydrogels, cleavage of amide bonds occur at a much higher rate. The fibrillar structure of D-coll hydrogel results in a more pronounced breakdown of the gel network and dissolution of collagen peptides. The results from this work will improve the understanding of enzymatic degradation and the resulting bioabsorption of collagen materials used in drug delivery systems and scaffolds.
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spelling pubmed-77096302020-12-03 Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum Ng, Hon Wei Zhang, Yi Naffa, Rafea Prabakar, Sujay Gels Communication Collagen-based hydrogels are investigated extensively in tissue engineering for their tunable physiochemical properties, biocompatibility and biodegradability. However, the effect of the integrity of the collagen triple helical structure on biodegradability is yet to be studied. In this study, we monitored the degradation of intact collagen (C-coll) and hydrolyzed collagen (D-coll) hydrogels in collagenase Clostridium histolyticum to understand their degradation process. Our results show that when peptides are present on the surface of the fibrils of D-coll hydrogels, cleavage of amide bonds occur at a much higher rate. The fibrillar structure of D-coll hydrogel results in a more pronounced breakdown of the gel network and dissolution of collagen peptides. The results from this work will improve the understanding of enzymatic degradation and the resulting bioabsorption of collagen materials used in drug delivery systems and scaffolds. MDPI 2020-11-27 /pmc/articles/PMC7709630/ /pubmed/33260949 http://dx.doi.org/10.3390/gels6040046 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Ng, Hon Wei
Zhang, Yi
Naffa, Rafea
Prabakar, Sujay
Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title_full Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title_fullStr Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title_full_unstemmed Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title_short Monitoring the Degradation of Collagen Hydrogels by Collagenase Clostridium histolyticum
title_sort monitoring the degradation of collagen hydrogels by collagenase clostridium histolyticum
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7709630/
https://www.ncbi.nlm.nih.gov/pubmed/33260949
http://dx.doi.org/10.3390/gels6040046
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