Phase transition and elasticity of protein-based hydrogels

J. Lee, C. W. Macosko, D. W. Urry

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Reported are specific materials characterizations of three protein-based polymers comprised of repeating pentapeptide sequences, namely (GVGVP)251, (GVGIP)260 and (GVGVP GVGVP GEGVP GVGVP GVGVP GVGVP)n](GVGVP) where G = glycine, V = valine, P = proline, I = isoleucine, and E = glutamic acid, which had been previously prepared and γ-irradiation cross-linked into elastic matrices. These polymers exhibit a hydrophobic folding and assembling transition on raising the temperature above a critical temperature, designated by Tt. Their equilibrium swelling ration, uniaxial tensile and dynamic shear behavior were studied. The effect of the transition on swelling and mechanical properties was demonstrated. Equilibrium swelling ratio below the transition temperature decreased with the increase of γ-irradiation dose. Above the transition temperature, hysteresis and frequency dependence were found in tensile loading-unloading tests and dynamic shear measurements, respectively. The rubber elasticity theory of random chain networks was applied to the data only below the transition temperature, where they may properly be considered random network hydrogels, to estimate molecular weight between cross-links and the Flory-Huggins interaction parameter.

Original languageEnglish (US)
Pages (from-to)229-242
Number of pages14
JournalJournal of Biomaterials Science, Polymer Edition
Issue number2
StatePublished - Jun 19 2001


  • Hydrogel
  • Hydrophobic hydration
  • Polypeptide
  • Protein-based polymer

Fingerprint Dive into the research topics of 'Phase transition and elasticity of protein-based hydrogels'. Together they form a unique fingerprint.

Cite this