自愈水凝胶
化学
生物材料
蛋白质工程
纤维
组织工程
生物物理学
酪氨酸
三螺旋
成纤维细胞
生物高聚物
生物化学
体外
生物
立体化学
高分子化学
有机化学
遗传学
酶
聚合物
作者
Akilandeswari Gopalan,Vijayakumar Varshashankari,Shalini Muthusamy,Mayilvahanan Aarthy,Karthigeyan Thamizhvani,Jebakumar Mercyjayapriya,Sundarapandian Ashokraj,Pachaiyappan Mohandass,Suresh Prem,Niraikulam Ayyadurai
摘要
Bacterial collagen, produced via recombinant DNA methods, offers advantages including consistent purity, customizable properties, and reduced allergy potential compared to animal-derived collagen. Its controlled production environment enables tailored features, making it more sustainable, non-pathogenic, and compatible with diverse applications in medicine, cosmetics, and other industries. Research has focused on the engineering of collagen-like proteins to improve their structure and function. The study explores the impact of introducing tyrosine, an amino acid known for its role in fibril formation across diverse proteins, into a newly designed bacterial collagen-like protein (Scl2), specifically examining its effect on self-assembly and fibril formation. Biophysical analyses reveal that the introduction of tyrosine residues didn't compromise the protein's structural stability but rather promoted self-assembly, resulting in the creation of nanofibrils-a phenomenon absent in the native Scl2 protein. Additionally, stable hydrogels are formed when the engineered protein undergoes di-tyrosine crosslinking under light exposure. The hydrogels, shown to support cell viability, also facilitate accelerated wound healing in mouse fibroblast (NIH/3T3) cells. These outcomes demonstrate that the targeted inclusion of functional residues in collagen-like proteins enhances fibril formation and facilitates the generation of robust hydrogels using riboflavin chemistry, presenting promising paths for research in tissue engineering and regenerative medicine.
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