Abstract
Because of the bioactivity and biocompatibility of protein-based gels and the reversible nature of bonds between associating coiled coils, these materials demonstrate a wide spectrum of potential applications in targeted drug delivery, tissue engineering, and regenerative medicine. The kinetics of rearrangement (association and dissociation) of the physical bonds between chains has been traditionally studied in shear relaxation tests and small-amplitude oscillatory tests. A characteristic feature of recombinant protein gels is that chains in the polymer network are connected by temporary bonds between the coiled coil complexes and permanent cross-links between functional groups of amino acids. A simple model is developed for the linear viscoelastic behavior of protein-based gels. Its advantage is that, on the one hand, the model only involves five material parameters with transparent physical meaning and, on the other, it correctly reproduces experimental data in shear relaxation and oscillatory tests. The model is applied to study the effects of temperature, the concentration of proteins, and their structure on the viscoelastic response of hydrogels.
Highlights
The design, preparation, and analysis of the mechanical response and physical and biological properties of hydrogels based on recombinant proteins and synthetic peptides have attracted considerable attention in the past decade [1,2,3,4,5,6,7,8]
An advantage of recombinant proteins when compared with those extracted from natural sources is that (i) concerns that are caused by disease transmission, immunogenic responses, and large batch-to-batch variability do not arise for these materials [18], while (ii) their physical properties and biological activity can be modulated by changing the biosynthesis conditions [19]
Material parameters in the governing equations are determined by matching observations in relaxation and oscillatory tests when this coefficient is small (Figures 4–6)
Summary
The design, preparation, and analysis of the mechanical response and physical and biological properties of hydrogels based on recombinant proteins and synthetic peptides have attracted considerable attention in the past decade [1,2,3,4,5,6,7,8]. An advantage of recombinant proteins when compared with those extracted from natural sources is that (i) concerns that are caused by disease transmission, immunogenic responses, and large batch-to-batch variability do not arise for these materials [18], while (ii) their physical properties and biological activity can be modulated by changing the biosynthesis conditions [19]. Because of the bioactivity of protein- and peptide-based gels and their superior mechanical and physical properties (that resemble those of the extracellular matrix), these materials have shown promise for applications in targeted drug delivery [20] and localized viral gene delivery [21], bioimaging [22], biosensing [23], bioelectronics [24], vaccine 4.0/).
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