纤维蛋白
化学
Ⅰ型胶原
生物物理学
纤维蛋白原
细胞外基质
自愈水凝胶
凝血酶
化学工程
生物化学
高分子化学
血小板
免疫学
医学
病理
工程类
生物
作者
Kun Wang,Marie Camman,Gervaise Mosser,Bernard Haye,Léa Trichet,Thibaud Coradin
出处
期刊:Molecules
[MDPI AG]
日期:2022-03-24
卷期号:27 (7): 2099-2099
被引量:2
标识
DOI:10.3390/molecules27072099
摘要
Fibrin-Type I collagen composite gels have been widely studied as biomaterials, in which both networks are usually formed simultaneously at a neutral pH. Here, we describe a new protocol in which mixed concentrated solutions of collagen and fibrinogen were first incubated at acidic pH to induce fibrinogen gel formation, followed by a pH change to neutral inducing collagen fiber formation. Thrombin was then added to form fibrin-collagen networks. Using this protocol, mixed gels containing 20 mg.mL-1 fibrin and up to 10 mg.mL-1 collagen could be prepared. Macroscopic observations evidenced that increasing the content of collagen increases the turbidity of the gels and decreases their shrinkage during the fibrinogen-to-fibrin conversion. The presence of collagen had a minor influence on the rheological properties of the gels. Electron microscopy allowed for observation of collagen fibers within the fibrin network. 2D cultures of C2C12 myoblasts on mixed gels revealed that the presence of collagen favors proliferation and local alignment of the cells. However, it interferes with cell differentiation and myotube formation, suggesting that further control of in-gel collagen self-assembly is required to elaborate fully functional biomaterials.
科研通智能强力驱动
Strongly Powered by AbleSci AI