弹性蛋白
伤口愈合
体内
融合蛋白
化学
体外
成纤维细胞
细胞生物学
肽
原弹性蛋白
重组DNA
生物化学
生物
病理
医学
免疫学
生物技术
基因
作者
Yingli Chen,Yuanyuan Wu,Fengmin Xiong,Wei Yu,Tingting Wang,Jianping Xiong,Luping Zhou,Fei Hu,Xianlong Ye,Jingyu Yan
出处
期刊:Molecules
[MDPI AG]
日期:2023-09-23
卷期号:28 (19): 6773-6773
被引量:2
标识
DOI:10.3390/molecules28196773
摘要
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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