A review of protein hydrogels: Protein assembly mechanisms, properties, and biological applications

Modelling network formation in folded protein hydrogels by cluster aggregation kinetics

“…Gel structures which yield percolating pore networks (e.g. low monomer volume fractions) 90 are important for applications where diffusion through the gel is important, such as in drug delivery and nutrient accessibility for in cell-seeded gels 40,[92][93][94][95][96][97][98] .…”

“…low monomer volume fractions) 90 are important for applications where diffusion through the gel is important, such as in drug delivery and nutrient accessibility for in cellseeded gels. 40,[92][93][94][95][96][97][98] Pore size and distribution are important considerations in tissue engineering, for example where certain cell types need pores of particular sizes for effective growth and tissue regeneration. 99,100 Being able to control and reproduce the properties of porous gel structure is important for regulating seeded cell properties and behaviour, including proliferation, migration, differentiation and phenotypic variation.…”

“…However, as covered comprehensively in the recent review article by Stradner et al 13 , in the right circumstances, where (quasi)spherical globular proteins retain their tertiary conformation 38,39 , this approach is appropriate and can bring valuable insight into the mechanisms leading to observed structures and mechanics of protein hydrogels across the lengthscales. Indeed, a growing field has emerged which exploits folded globular proteins for the creation of hydrogels, using irreversible crosslinking to control network formation 40,41 . For example, the maximum coordination of folded proteins in gels (defined as the maximum allowed number of chemical crosslinks per domain) can be controlled by tuning the number of site-specific binding residues on the surface of the proteins 42 .…”

“…Indeed, a growing field has emerged which exploits folded globular proteins for the creation of hydrogels, using irreversible crosslinking to control network formation. 40,41 For example, the maximum coordination of folded proteins in gels (defined as the maximum allowed number of chemical crosslinks per domain) can be controlled by tuning the number of site-specific binding residues on the surface of the proteins. 42 Such systems lend themselves well to a colloidbased modelling approach, and there is now a growing body of literature on the assembly, rheology and structure of such hydrogels.…”

Nanomaterial-based biohybrid hydrogel in bioelectronics

“…Thus, biohybrid hydrogel developed by combination of nanomaterials and hydrogels can suggest the solution to overcome these limitations of conventional hydrogels through the offer of the synergic effect based on the excellent properties from each component such as the biocompatibility from hydrogel and the conductivity from nanomaterials [ 21 , 22 ]. For example, nanomaterials show advantages in bioelectronics applications, increasing conductivity and structural stability as well as improving biocompatibility by combining with biomaterials such as peptides, nucleic acids, and enzymes [ 23 , 24 ]. In addition, nanomaterials can be utilized to address the limitations of hydrogels by combining with them.…”