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

Abstract 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-res...

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Bibliographic Details
Published in:Biomaterials 2011-11, Vol.32 (33), p.8462-8473
Main Authors: Truong, My Y, Dutta, Naba K, Choudhury, Namita R, Kim, Misook, Elvin, Christopher M, Nairn, Kate M, Hill, Anita J
Format: Article
Language:English
Subjects:
Advanced Basic Science
Amino Acid Sequence
Biomimetic protein
Biopolymers
Calorimetry, Differential Scanning
Crystallization
Dentistry
Elasticity
Hydration
Hydrogel
Insect Proteins - chemistry
Kinetics
Molecular Sequence Data
Rec1-resilin
Rheological properties
Sequence Homology, Amino Acid
Sorption isotherm
Thermogravimetry
Viscosity
Water - chemistry
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Summary:Abstract 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  cm2  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 ( Tg ) 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 (
ISSN:0142-9612
1878-5905
DOI:10.1016/j.biomaterials.2011.07.064