Amyloid‐Based Albumin Hydrogels

Abstract

Amyloid fibrils may serve as building blocks for the preparation of novel hydrogel materials from abundant, low‐cost, and biocompatible polypeptides. This work presents the formation of physically cross‐linked, self‐healing hydrogels based on bovine serum albumin at room temperature through a straightforward disulfide reduction step induced by tris (2‐carboxyethyl) phosphine hydrochloride. The structure and surface charge of the amyloid‐like fibrils is determined by the pH of the solution during self‐assembly, giving rise to hydrogels with distinct physicochemical properties. The hydrogel surface can be readily functionalized with the extracellular matrix protein fibronectin and supports 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.

Functional Amyloids: The Biomaterials of Tomorrow?

“…However, bio-based, specifically protein-and peptide-based hydrogels may be viable alternatives. [8,[40][41][42][43] While less well-defined compared to synthetic hydrogels, naturally derived hydrogels have macromolecular properties that more closely resemble those of tissue extracellular matrix than polymer hydrogels do. Furthermore, successful cell growth and differentiation are often correlated with proper cell adhesion and signaling, which are much easier achieved with protein and peptide-based hydrogels.…”

Research progress on albumin-based hydrogels: Properties, preparation methods, types and its application for antitumor-drug delivery and tissue engineering

“…There are numerous drug-binding sites on albumin, two main drug-binding sites for albumin are Sudlow site I and Sudlow site II, and albumin can bind more drugs when these two sites are sufficiently exposed (Rong et al, 2022;Bercea et al, 2023) Biological properties Low allergenicity Protein amyloid fibrils are derived from natural proteins, which are more biocompatible and have a lower probability of causing allergic reactions (Willbold et al, 2021). Amyloid fibrils can be used as building blocks for novel albumin-based hydrogel materials that are biocompatible, low cost and hypoallergenic (Diaz and Missirlis, 2022) High biological activity Compared to protein monomers, some amyloid fibrils have stronger antioxidant and antibacterial activity. Some amino acids have high antioxidant activity, such as cysteine, methionine, tryptophan, tyrosine and phenylalanine, and these amino acids are also often involved in the formation of amyloid fibrils.…”

3D printable, injectable amyloid-based composite hydrogel of bovine serum albumin and aloe vera for rapid diabetic wound healing

“…Having achieved significant accomplishments in academic research and commercialization over the past decade, hydrogels have emerged as a captivating feature of modern materials science. 1,2 Researchers and engineers have been captivated by the distinct and varied attributes exhibited by these hydrogels, which offer immense potential for numerous interesting applications. Composed of a three-dimensional network of water-soluble polymers, hydrogels can absorb and retain large amounts of water.…”

“…32 Such amyloid-based hydrogels possess remarkable biocompatibility and controlled biodegradability due to their highly ordered structure and the multifunctional moieties of the protein molecule. 32 Recently, researchers have demonstrated the in vitro formation of amyloid fibril-based hydrogels using diverse proteins such as bovine serum albumin (BSA), 33 lysozyme, 34 lactoglobulin, 35 etc. In particular, BSA has received a lot of attention due to its low cost and biocompatibility.…”

“…30,31 Amyloid fibrils are a good candidate for nanobiotechnological applications because they tend to form hydrogels with excellent stability and tuneable mechanical characteristics under specific physicochemical conditions. 32 Such amyloid-based hydrogels possess remarkable biocompatibility and controlled biodegradability due to their highly ordered structure and the multifunctional moieties of the protein molecule. 32 Recently, researchers have demonstrated the in vitro formation of amyloid fibril-based hydrogels using diverse proteins such as bovine serum albumin (BSA), 33 lysozyme, 34 lactoglobulin, 35 etc.…”