Functionalization of Recombinant Amelogenin Nanospheres Allows Their Binding to Cellulose Materials

Samuel J. Butler, Leif Bülow, Johan Bonde

Research output: Contribution to journalArticlepeer-review

4 Citations (SciVal)

Abstract

Protein engineering to functionalize the self-assembling enamel matrix protein amelogenin with a cellulose binding domain (CBD) is used. The purpose is to examine the binding of the engineered protein, rh174CBD, to cellulose materials, and the possibility to immobilize self-assembled amelogenin nanospheres on cellulose. rh174CBD assembled to nanospheres ≈35 nm in hydrodynamic diameter, very similar in size to wild type amelogenin (rh174). Uniform particles are formed at pH 10 for both rh174 and rh174CBD, but only rh174CBD nanospheres showes significant binding to cellulose (Avicel). Cellulose binding of rh174CBD is promoted when the protein is self-assembled to nanospheres, compared to being in a monomeric form, suggesting a synergistic effect of the multiple CBDs on the nanospheres. The amount of bound rh174CBD nanospheres reached ≈15 mg/g Avicel, which corresponds to 4.2 to 6.3 × 10−7 mole/m2. By mixing rh174 and rh174CBD, and then inducing self-assembly, composite nanospheres with a high degree of cellulose binding can be formed, despite a lower proportion of rh174CBD. This demonstrates that amelogenin variants like rh174 can be incorporated into the nanospheres, and still retain most of the binding to cellulose. Engineered amelogenin nanoparticles can thus be utilized to construct a range of new cellulose based hybrid materials, e.g. for wound treatment.

Original languageEnglish
Pages (from-to)1343-1351
Number of pages9
JournalBiotechnology Journal
Volume11
Issue number10
DOIs
Publication statusPublished - 2016 Oct 1

Subject classification (UKÄ)

  • Medical Biotechnology

Keywords

  • Amelogenin
  • Biomaterial
  • Cellulose
  • Nanoparticles
  • Protein

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