Improvement of collagen self-assembly and thermal stability in the presence of trehalose

Collagen self-assembly into fibrous structures is a phenomenon that attracts wide attention in the biomedical and tissue engineering material fields. However, collagen's shortcoming of low thermal stability limits its application. Trehalose, a well-known compatible osmolyte, can stabilize proteins against various denaturing conditions. Herein, the effect of trehalose on the self-assembly and conformational stability of collagen was explored. The effect of trehalose on self-assembly was studied with turbidity, chloramine T assay, rheology, SEM and TEM characterizations. Circular dichroism (CD) was used to monitor the impact of trehalose on the triple helical conformation stability of collagen. The obtained experimental results reveal that trehalose could (1) accelerate the self-assembly kinetics and improve the self-assembly degree of collagen and the mechanical properties of the resulting hydrogels, but has no impact on the microstructure of the resulting collagen fibrils, and (2) increase the thermal stability of collagen. Both are desirable for the industrial application of collagen-based materials. Furthermore, the MTT assay and cell morphology characterization suggest that trehalose has no effect on the cytocompatibility of collagen materials.

Automated summary

Trehalose has a promoting effect on the self-assembly and conformational stability of collagen, without affecting the microstructure of collagen fibrils. It also increases the thermal stability of collagen and has no effect on the cytocompatibility of collagen materials.