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Repairing tubular tissues—the trachea, the esophagus, urinary and gastrointestinal tracts, and the circulatory system—from trauma or severe pathologies that require resection, calls for new, more effective graft materials. Currently, the relatively narrow family of materials available for these applications relies on synthetic polymers that fail to reproduce the biological and physical cues found in native tissues. Mimicking the structure and the composition of native tubular tissues to elaborate functional grafts is expected to outperform the materials currently in use, but remains one of the most challenging goals in the field of biomaterials. Despite their apparent diversity, tubular tissues share extensive compositional and structural features. Here, we assess the current state of the art through a dual layer model, reducing each tissue to an inner epithelial layer and an outer muscular layer. Based on this model, we examine the current strategies developed to mimic each layer and we underline how each fabrication method stands in providing a biomimetic material for future clinical translation. The analysis provided here, addressed to materials chemists, biomaterials engineers and clinical staff alike, sets new guidelines to foster the elaboration of new biomimetic materials for effective tubular tissue repair. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

We report on elasticity measurements in neuronlike cells using picosecond acoustics pump and probe spectroscopy. The stimulated Brillouin oscillations were mapped in PC12 cells to reveal their internal elastic structure. Thanks to a Pearson correlation coefficient mapping, different areas could be distinguished. The nucleus material shows a bulk modulus equal to 12.9 GPa in the case of a dry cell. Attenuation of the Brillouin signature gives access to dynamical longitudinal viscosity equal to 10.6 mPa ⋅ s, one order of magnitude higher than that of water. The modulus considerably drops to 2.6 GPa in the most physiologically relevant case of a hydrated cell. [ABSTRACT FROM AUTHOR]

Type I collagen and fibrin are two essential proteins in tissue regeneration and have been widely used for the design of biomaterials. While they both form hydrogels via fibrillogenesis, they have distinct biochemical features, structural properties and biological functions which make their combination of high interest. A number of protocols to obtain such mixed gels have been described in the literature that differ in the sequence of mixing/addition of the various reagents. Experimental and modelling studies have suggested that such co-gels consist of an interpenetrated structure where the two proteins networks have local interactions only. Evidences have been accumulated that immobilized cells respond not only to the overall structure of the co-gels but can also exhibit responses specific to each of the proteins. Among the many biomedical applications of such type I collagen-fibrin mixed gels, those requiring the co-culture of two cell types with distinct affinity for these proteins, such as vascularization of tissue engineering constructs, appear particularly promising., Competing Interests: The authors declare no conflict of interest

Silanization of biomacromolecules has emerged as a fruitful approach to prepare hybrid biohydrogels. However, very little is known about interactions between organosilanes and biopolymers in solution. Here we focused on fibrin, a protein of interest in the biomedical field, whose self-assembly process and resulting gel structure are highly sensitive to experimental conditions. Three main silanes were selected to decipher the relative influence of the silanol groups and organic functions. Whereas no protein denaturation was observed, silanes bearing hydrophobic groups had a surfactant-like behavior and could improve the dispersion of fibrinogen molecules, impacting gel formation kinetics and rheological properties. 3D cultures of myoblasts evidenced that organosilanes could promote or impede cell proliferation, suggesting interactions of silanols with fibrin. These results demonstrate that the two sides of the coin of organosilane reactivity are relevant at different stages of fibrin gel formation and must be considered for future development of hybrid biomaterials.