Construction and expression of recombinant human elastin with biological activities: effect of wound healing in vitro and in vivo.

Elastin (ELN) is a key extracellular matrix protein that is crucial for the elasticity of many vertebrate tissues. Due to the low solubility of the natural elastin, its application in research has been limited, and soluble elastin derivatives has a wider range of applications. At present, the use of prokaryotic expression systems to obtain recombinant protein has the advantages of low cost, controllable sequence, and low immunogenicity, making it the optimal method for large-scale protein production. To address existing limitations, in this work, we designed and constructed two recombinant human elastins, which were expressed, purified, and then evaluated for activity through cell proliferation, migration and antioxidant assays. The EL1 and RE1 significantly promoted the proliferation and migration of 3T3 cells. Studies on a mouse skin wound model demonstrated that two recombinant elastins likely promotes wound healing by mitigating inflammatory responses, accelerating collagen deposition, and regulating CD31 and α-SMA factors to enhance angiogenesis. This study demonstrates two new recombinant human elastins with good biological activity and can promote wound healing in mice, highlighting its potential as a promising biomolecular therapeutic strategy for skin wound repair.