Bionanocomposites: Differential effects of cellulose nanocrystals on protein diblock copolymers

Jennifer S. Haghpanah, Raymond Tu, Sandra Da Silva, Deng Yan, Silvana Mueller, Christoph Weder, E. Johan Foster, Iulia Sacui, Jeffery W. Gilman, Jin Kim Montclare

Research output: Contribution to journalArticlepeer-review


We investigate the effects of mixing a colloidal suspension of tunicate-derived cellulose nanocrystals (t-CNCs) with aqueous colloidal suspensions of two protein diblock copolymers, EC and CE, which bear two different self-assembling domains (SADs) derived from elastin (E) and the coiled-coil region of cartilage oligomeric matrix protein (C). The resulting aqueous mixtures reveal improved mechanical integrity for the CE+t-CNC mixture, which exhibits an elastic gel network. This is in contrast to EC+t-CNC, which does not form a gel, indicating that block orientation influences the ability to interact with t-CNCs. Surface analysis and interfacial characterization indicate that the differential mechanical properties of the two samples are due to the prevalent display of the E domain by CE, which interacts more with t-CNCs leading to a stronger network with t-CNCs. On the other hand, EC, which is predominantly C-rich on its surface, does not interact as much with t-CNCs. This suggests that the surface characteristics of the protein polymers, due to folding and self-assembly, are important factors for the interactions with t-CNCs, and a significant influence on the overall mechanical properties. These results have interesting implications for the understanding of cellulose hydrophobic interactions, natural biomaterials and the development of artificially assembled bionanocomposites.

Original languageEnglish (US)
Pages (from-to)4360-4367
Number of pages8
Issue number12
StatePublished - Dec 9 2013

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


Dive into the research topics of 'Bionanocomposites: Differential effects of cellulose nanocrystals on protein diblock copolymers'. Together they form a unique fingerprint.

Cite this