Bioinspired Amyloid Fibril‐Based Hydrogel with Engineering Programable Functionalities for Diverse Applications

Abstract

Natural proteins display organized hierarchical structures and tailored functionalities that cannot be achieved by synthetic approaches, highlighting the increased interest in developing protein‐based materials. Protein self‐assembly allows fabricating sophisticated supramolecular structures from relatively simple building blocks, a strategy naturally employed by amyloid proteins and intrinsically disordered proteins. However, the design of self‐assembled bioinspired materials with multi functionalities is still challenging. Inspired by the natural self‐assembly proteins (such as mussel foot proteins and amyloid proteins), a temperature‐inducible engineering programable hydrogel‐like amyloid nanostructure is developed by using a genetically modular fusion approach. The resulting hydrogel‐like assemblies display outstanding adhesive capacity, high stability, and broad substrate universality. The employed SpyCatcher/SpyTag system allows modifying the hydrogel‐like assemblies with any functional proteins of interest. Owing to their strong adhesive capacity and functional flexibility, such amyloid fibril‐based hydrogel shows advantages in the immobilization of diverse enzymes for highly efficient biocatalysis, fabrication of multi‐layered functional coatings, and construction of functionalized 3D scaffold for cell culture. Overall, a modular and straightforward approach is established to obtain a genetically programable nanostructure platform. The novel hydrogel‐like assemblies described here may be potentially applied to but not limited to synthetic biology, surface/interface engineering, and tissue engineering.

Silver Mineralized Protein Hydrogel with Intrinsic Cell Proliferation Promotion and Broad‐Spectrum Antimicrobial Properties for Accelerated Infected Wound Healing

“…We have previously developed a modular approach to fabricate adhesive amyloid‐based hydrogel by fusing a soft amyloid core to a short mussel foot protein mimetic peptide. [ 24 ] In order to further engineer the adhesive capacity of such system, we fused the soft amyloid core of Sup35 prion protein (Sup35‐SAC), an amyloid fibrils‐forming peptide, to an L‐DOPA enriched full‐length adhesive protein Perna viridis foot protein 5 (Pvfp5) through a flexible linker (SG 3 SG 2 S), resulting in a fusion protein Pvfp5‐Sup35 ( Figure a; and Tables S1 and S2, Supporting Information). Pvfp5 is an adhesive protein containing 82 amino acids, secreted from the foot‐gland of Perna viridis and enriched with L‐DOPA and charged amino acids, which endows Perna viridis with high adhesion to rocks under seawater.…”

“…The resulting hydrogel not only exhibits excellent mechanical properties and biocompatibility but also can be fabricated into functionalized scaffolds for improving mammalian cell proliferation. [ 24 ] In this study, we rationally construct a new fusion protein by replacing the short mussel foot protein mimetics with full‐length Perna viridis foot protein 5 (Pvfp5), resulting in a new fusion Pvfp5‐Sup35 (Figure 1c). The Pvfp5 domain is a typical mussel adhesive protein enriched with L‐DOPA, consists of 82 residues and displays a tandem EGF‐like module structure, showing high potential in tissue bioadhesive.…”

“…[23] In our previous study, we developed a modular strategy to fabricate a functionable building block by fusing a mussel foot protein mimetic peptide to a soft amyloid core sequence. [24] The soft amyloid cores (SACs) are short sequences within the large prion domain that suffice to nucleate their self-assembly reaction but allow the appended functional proteins to display native structure and functionality in the fusions. [25,26,27,28] The triple fusion protein can self-assemble into adhesive amyloid-based hydrogels (Figure 1b).…”