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

Truong, My Y., Dutta, Naba K., Choudhury, Namita R., Kim, Misook, Elvin, Christopher M., Nairn, Kate M. and Hill, Anita J. (2011) The effect of hydration on molecular chain mobility and the viscoelastic behavior of resilin-mimetic protein-based hydrogels. Biomaterials, 32 33: 8462-8473. doi:10.1016/j.biomaterials.2011.07.064


Author Truong, My Y.
Dutta, Naba K.
Choudhury, Namita R.
Kim, Misook
Elvin, Christopher M.
Nairn, Kate M.
Hill, Anita J.
Title The effect of hydration on molecular chain mobility and the viscoelastic behavior of resilin-mimetic protein-based hydrogels
Journal name Biomaterials   Check publisher's open access policy
ISSN 0142-9612
1878-5905
Publication date 2011-11-01
Sub-type Article (original research)
DOI 10.1016/j.biomaterials.2011.07.064
Volume 32
Issue 33
Start page 8462
End page 8473
Total pages 12
Place of publication Amsterdam, Netherlands
Publisher Elsevier BV
Collection year 2012
Language eng
Formatted 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 (<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.
Keyword Biomimetic protein
Rec1-resilin
Rheological properties
Hydrogel
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: UQ Centre for Clinical Research Publications
Non HERDC
School of Chemistry and Molecular Biosciences
 
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Citation counts: TR Web of Science Citation Count  Cited 27 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 19 Oct 2011, 21:54:25 EST by Ms Misook Kim on behalf of School of Chemistry & Molecular Biosciences