Advanced

Functionalization of Recombinant Amelogenin Nanospheres Allows Their Binding to Cellulose Materials

Butler, Samuel J.; Bülow, Leif LU and Bonde, Johan LU (2016) In Biotechnology Journal 11(10). p.1343-1351
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... (More)

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.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amelogenin, Biomaterial, Cellulose, Nanoparticles, Protein
in
Biotechnology Journal
volume
11
issue
10
pages
9 pages
publisher
John Wiley & Sons
external identifiers
  • scopus:84989897320
  • wos:000388304600011
ISSN
1860-6768
DOI
10.1002/biot.201600381
language
English
LU publication?
yes
id
24f17e71-163d-40f8-8a11-e1890e65ef4e
date added to LUP
2016-10-20 10:19:47
date last changed
2017-10-22 05:20:46
@article{24f17e71-163d-40f8-8a11-e1890e65ef4e,
  abstract     = {<p>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<sup>−7</sup> mole/m<sup>2</sup>. 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.</p>},
  author       = {Butler, Samuel J. and Bülow, Leif and Bonde, Johan},
  issn         = {1860-6768},
  keyword      = {Amelogenin,Biomaterial,Cellulose,Nanoparticles,Protein},
  language     = {eng},
  month        = {10},
  number       = {10},
  pages        = {1343--1351},
  publisher    = {John Wiley & Sons},
  series       = {Biotechnology Journal},
  title        = {Functionalization of Recombinant Amelogenin Nanospheres Allows Their Binding to Cellulose Materials},
  url          = {http://dx.doi.org/10.1002/biot.201600381},
  volume       = {11},
  year         = {2016},
}