This study reports in vitro reconstitution of collagen-alginate blends with a wide range of algi-nate/collagen ratios, aiming at revealing the nanostructured fibrillar networks assembled at high collagen concentrations. The aggregation states of collagen monomeric solutions at varying concentrations from 1 to 7 mg/ml, in the absence or presence of alginate, were examined by using scanning electron microscopy and atomic force microscopy. Compared with collagen, the blends with increasing alginate/collagen ratios assembled into looser three-dimensional fibrillar networks interlaced by larger twisted fibrils which were irregular and dense aggregates of smaller fibrils with the normal banding periodicity. Typical turbidimet-ric assays revealed the different kinetics in presence of alginate and alginate-eluted quantitation further confirming the capturing of alginate in the collagen-alginate fibrillar networks. The electrostatic com-plexation between collagen and alginate was postulated to play a crucial role in this abnormal aggregation of collagen-alginate blends.
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