From Protein Building Blocks to Functional Materials

Abstract

Proteins are the fundamental building blocks for high-performance materials in nature. Such materials fulfill structural roles, as in the case of silk and collagen, and can generate active structures including the cytoskeleton. Attention is increasingly turning to this versatile class of molecules for the synthesis of next-generation green functional materials for a range of applications. Protein nanofibrils are a fundamental supramolecular unit from which many macroscopic protein materials are formed. In this Review, we focus on the multiscale assembly of such protein nanofibrils formed from naturally occurring proteins into new supramolecular architectures and discuss how they can form the basis of material systems ranging from bulk gels, films, fibers, micro/nanogels, condensates, and active materials. We review current and emerging approaches to process and assemble these building blocks in a manner which is different to their natural evolutionarily selected role but allows the generation of tailored functionality, with a focus on microfluidic approaches. We finally discuss opportunities and challenges for this class of materials, including applications that can be involved in this material system which consists of fully natural, biocompatible, and biodegradable feedstocks yet has the potential to generate materials with performance and versatility rivalling that of the best synthetic polymers.

Liquid–Liquid Phase‐Separated Systems from Reversible Gel–Sol Transition of Protein Microgels

“…Previously we have reported different crosslinking regimes, physical or enzymatic, for the templating of protein microgels. [ 4,20,21 ] Transglutaminase solution was used to enzymatically crosslink the physically crosslinked microrods from their surfaces, and this enzyme catalyses the formation of covalent N ε‐(γ‐glutamyl) lysine amide bonds between the gelatin strands to form a permanent network of polypeptides (Figure , Supporting Information). [ 4,20,22 ] The physically and enzymatically crosslinked microrods did not undergo a gel–sol transition when heated to 37 °C, as they were more thermostable (Figure , Supporting Information) than the physically crosslinked microgels (Figure 2a).…”

Effect of Chitosan Deacetylation on Its Affinity to Type III Collagen: A Molecular Dynamics Study

“…The collagen triple helices form the "building blocks" of tissues, namely fibrils and fibers. Furthermore, the collagen nanofibrils can be used for obtaining various functional materials (e.g., gels, films, and microgels) [1]. Interestingly, the molecular dynamics (MD) calculations results reported by Mathavi et al (2019) [2] showed that the collagen self-assemblies are stabilized by the interchain water-mediated hydrogen bonds (H-bonds).…”

Biohybrid Nanocellulose–Lysozyme Amyloid Aerogels via Electrostatic Complexation

“… 29 , 30 In general, protein amyloids are extremely versatile, due to the functional diversity in the protein/peptide moieties they are formed from; this has led to their application in areas such as catalysis, filtration, drug delivery, and biomimetic functional materials. 31 , 32 To this end, lysozyme has gained particular interest for its ability to rapidly form amyloid aggregates with broad spectrum antibacterial resistance. 33 − 36 This is of particular interest as lysozyme in its native form demonstrates little to no antibacterial efficacy against Gram-negative bacteria.…”