Governing the aggregation of type I collagen mediated through β-cyclodextrin.

The effect of carbohydrates on collagen self-assembly behavior has been widely investigated because of their regulation on collagen fibrogenesis in vivo. In this paper, β-cyclodextrin (β-CD) was selected as an external disturbance to explore its intrinsic regulating mechanism on collagen self-assembly. The results of fibrogenesis kinetics indicated that β-CD had a bilateral regulation on collagen self-aggregation process, which was closely related to the content of β-CD: collagen protofibrils with low β-CD content were less aggregated compared to collagen protofibrils with high β-CD content. However, typical periodic stripes of ~67 nm on collagen fibrils were observed from transmission electron microscope (TEM), indicating that β-CD did not disturb the lateral arrangement of collagen molecules to form a 1/4 staggered structure. Correspondingly, the degree of aggregation of collagen self-assembled fibrils was closely correlated with the addition of β-CD content, as confirmed by field emission scanning electron microscopy (FESEM) and atomic force microscope (AFM). In addition, collagen/β-CD fibrillar hydrogel had good thermal stability and cytocompatibility. These results provide a better understanding of how to construct a structurally reliable collagen/β-CD fibrillar hydrogel as a biomedical material in a β-CD-regulated environment.