The effect of hydration on molecular chain mobility and the viscoelastic behavior of resilin-mimetic protein-based...

The outstanding rubber-like elasticity of resilin and resilin-mimetic proteins depends critically on the level of hydration. In this investigation, water vapor sorption and the role of hydration on the molecular chain dynamics and viscoelastic properties of resilin-mimetic protein, rec1-resilin is investigated in detail. The dynamic and equilibrium swelling behavior of the crosslinked protein hydrogels with different crosslink density are reported under various controlled environments. We propose three different stages of hydration; involving non-crystallizable water, followed by condensation or clustering of water around the already hydrated sites, and finally crystallizable water. The kinetics of water sorption for this engineering protein is observed to be comparable to hydrophilic polymers with a diffusion coefficient in the range of 10(-7) cm(2) s(-1). From the comparison between the absorption and desorption isotherms at a constant water activity, it has been observed that rec1-resilin exhibits sorption hysteresis only for the tightly bound water. Investigation of molecular mobility using differential scanning calorimetry, indicates that dehydrated crosslinked rec1-resilin is brittle with a glass transition temperature (T(g)) of >180 °C, which dramatically decreases with increasing hydration; and above a critical level of hydration rec1-resilin exhibits rubber-like elasticity. Nanoindentation studies show that even with little hydration (<10%), the mechanical properties of rec1-resilin gels change dramatically. Rheological investigations confirm that the equilibrium-swollen crosslinked rec1-resilin hydrogel exhibits outstanding elasticity and resilience of ∼ 92%, which exceeds that of any other synthetic polymer and biopolymer hydrogels.