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Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing
In the healing of wounds, human-like collagen (hCol) is essential. However, collagen-based composite dressings have poor stability in vivo, which severely limits their current therapeutic potential. Based on the above, we have developed a recombinant fusion protein named hCol-ELP, which consists of...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574607/ https://www.ncbi.nlm.nih.gov/pubmed/37836616 http://dx.doi.org/10.3390/molecules28196773 |
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author | Chen, Yingli Wu, Yuanyuan Xiong, Fengmin Yu, Wei Wang, Tingting Xiong, Jingjing Zhou, Luping Hu, Fei Ye, Xianlong Liang, Xinmiao |
author_facet | Chen, Yingli Wu, Yuanyuan Xiong, Fengmin Yu, Wei Wang, Tingting Xiong, Jingjing Zhou, Luping Hu, Fei Ye, Xianlong Liang, Xinmiao |
author_sort | Chen, Yingli |
collection | PubMed |
description | In the healing of wounds, human-like collagen (hCol) is essential. However, collagen-based composite dressings have poor stability in vivo, which severely limits their current therapeutic potential. Based on the above, we have developed a recombinant fusion protein named hCol-ELP, which consists of hCol and an elastin-like peptide (ELP). Then, we examined the physicochemical and biological properties of hCol-ELP. The results indicated that the stability of the hCol-ELP fusion protein exhibited a more compact and homogeneous lamellar microstructure along with collagen properties, it was found to be significantly superior to the stability of free hCol. The compound hCol-ELP demonstrated a remarkable capacity to induce the proliferation and migration of mouse embryo fibroblast cells (NIH/3T3), as well as enhance collagen synthesis in human skin fibroblasts (HSF) when tested in vitro. In vivo, hCol-ELP demonstrated significant enhancements in healing rate and a reduction in the time required for scab removal, thereby exhibiting a scar-free healing effect. The findings provide a crucial theoretical foundation for the implementation of an hCol-ELP protein dressing in fields associated with the healing of traumatic injuries. |
format | Online Article Text |
id | pubmed-10574607 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105746072023-10-14 Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing Chen, Yingli Wu, Yuanyuan Xiong, Fengmin Yu, Wei Wang, Tingting Xiong, Jingjing Zhou, Luping Hu, Fei Ye, Xianlong Liang, Xinmiao Molecules Article In the healing of wounds, human-like collagen (hCol) is essential. However, collagen-based composite dressings have poor stability in vivo, which severely limits their current therapeutic potential. Based on the above, we have developed a recombinant fusion protein named hCol-ELP, which consists of hCol and an elastin-like peptide (ELP). Then, we examined the physicochemical and biological properties of hCol-ELP. The results indicated that the stability of the hCol-ELP fusion protein exhibited a more compact and homogeneous lamellar microstructure along with collagen properties, it was found to be significantly superior to the stability of free hCol. The compound hCol-ELP demonstrated a remarkable capacity to induce the proliferation and migration of mouse embryo fibroblast cells (NIH/3T3), as well as enhance collagen synthesis in human skin fibroblasts (HSF) when tested in vitro. In vivo, hCol-ELP demonstrated significant enhancements in healing rate and a reduction in the time required for scab removal, thereby exhibiting a scar-free healing effect. The findings provide a crucial theoretical foundation for the implementation of an hCol-ELP protein dressing in fields associated with the healing of traumatic injuries. MDPI 2023-09-23 /pmc/articles/PMC10574607/ /pubmed/37836616 http://dx.doi.org/10.3390/molecules28196773 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Chen, Yingli Wu, Yuanyuan Xiong, Fengmin Yu, Wei Wang, Tingting Xiong, Jingjing Zhou, Luping Hu, Fei Ye, Xianlong Liang, Xinmiao Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title | Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title_full | Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title_fullStr | Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title_full_unstemmed | Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title_short | Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing |
title_sort | construction of a collagen-like protein based on elastin-like polypeptide fusion and evaluation of its performance in promoting wound healing |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574607/ https://www.ncbi.nlm.nih.gov/pubmed/37836616 http://dx.doi.org/10.3390/molecules28196773 |
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