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...

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Main Authors: Yingli Chen, Yuanyuan Wu, Fengmin Xiong, Wei Yu, Tingting Wang, Jingjing Xiong, Luping Zhou, Fei Hu, Xianlong Ye, Xinmiao Liang
Format: Article
Language:English
Published: MDPI AG 2023-09-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/28/19/6773
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author Yingli Chen
Yuanyuan Wu
Fengmin Xiong
Wei Yu
Tingting Wang
Jingjing Xiong
Luping Zhou
Fei Hu
Xianlong Ye
Xinmiao Liang
author_facet Yingli Chen
Yuanyuan Wu
Fengmin Xiong
Wei Yu
Tingting Wang
Jingjing Xiong
Luping Zhou
Fei Hu
Xianlong Ye
Xinmiao Liang
author_sort Yingli Chen
collection DOAJ
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.
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spelling doaj.art-41db9745a6fb475db0b10076e87e413a2023-11-19T14:45:23ZengMDPI AGMolecules1420-30492023-09-012819677310.3390/molecules28196773Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound HealingYingli Chen0Yuanyuan Wu1Fengmin Xiong2Wei Yu3Tingting Wang4Jingjing Xiong5Luping Zhou6Fei Hu7Xianlong Ye8Xinmiao Liang9Ganjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaGanjiang Chinese Medicine Innovation Center, Nanchang 330100, ChinaIn 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.https://www.mdpi.com/1420-3049/28/19/6773human-like collagen (hCol)elastin-like polypeptide (ELP)fusion proteinwound healing
spellingShingle Yingli Chen
Yuanyuan Wu
Fengmin Xiong
Wei Yu
Tingting Wang
Jingjing Xiong
Luping Zhou
Fei Hu
Xianlong Ye
Xinmiao Liang
Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing
Molecules
human-like collagen (hCol)
elastin-like polypeptide (ELP)
fusion protein
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 human-like collagen (hCol)
elastin-like polypeptide (ELP)
fusion protein
wound healing
url https://www.mdpi.com/1420-3049/28/19/6773
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