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Abstract

Amyloid fibrils may serve as building blocks for the preparation of novel hydrogel materials from abundant, low cost and biocompatible polypeptides. Here, we present the formation of physically cross-linked, self-healing hydrogels based on bovine serum albumin (BSA) at room temperature through a straightforward disulfide reduction step induced by tris (2-carboxyethyl) phosphine hydrochloride (TCEP). The structure and surface charge of the amyloid-like fibrils was determined by the pH of the solution during self-assembly, giving rise to hydrogels with distinct physicochemical properties. The hydrogel surface could be readily functionalized with the extracellular matrix protein fibronectin and supported cell adhesion, spreading and long-term culture. This study offers a simple, versatile and inexpensive method to prepare amyloid-based albumin hydrogels with potential applications in the biomedical field.