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Kinetic and thermodynamic study of the interactions between human carbonic anhydrase variants and polystyrene nanoparticles of different size

Assarsson, A. LU ; Nasir, I. LU ; Lundqvist, M. LU and Cabaleiro-Lago, C. LU (2016) In RSC Advances 6(42). p.35868-35874
Abstract

The activity and adsorption of three variants of human carbonic anhydrase (HCA) with similar topology but variation in charge and stability were studied in the presence of carboxyl-modified polystyrene nanoparticles of different sizes ranging from 25 nm to 114 nm. The balance of forces driving the adsorption of carbonic anhydrase variants is affected by the physicochemical properties of the protein and the nanoparticle size. All enzymes are totally inhibited upon adsorption due to the transition towards a molten globule like state that lacks enzymatic activity. The size of the particle affects the adsorption of human carbonic anhydrase I and N-terminal truncated human carbonic anhydrase II. Investigations on pH effects indicate that the... (More)

The activity and adsorption of three variants of human carbonic anhydrase (HCA) with similar topology but variation in charge and stability were studied in the presence of carboxyl-modified polystyrene nanoparticles of different sizes ranging from 25 nm to 114 nm. The balance of forces driving the adsorption of carbonic anhydrase variants is affected by the physicochemical properties of the protein and the nanoparticle size. All enzymes are totally inhibited upon adsorption due to the transition towards a molten globule like state that lacks enzymatic activity. The size of the particle affects the adsorption of human carbonic anhydrase I and N-terminal truncated human carbonic anhydrase II. Investigations on pH effects indicate that the size of the particle modulates the lateral interactions at the protein layer for these particular variants whose adsorption is mainly driven by electrostatic forces. A third variant, human carbonic anhydrase II, instead shows no strong influence of nanoparticle size which supports an adsorption process mainly driven by the hydrophobic effect.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
RSC Advances
volume
6
issue
42
pages
7 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:84965044010
ISSN
2046-2069
DOI
10.1039/c6ra06175c
language
English
LU publication?
yes
id
8fd42bec-a38c-4059-a526-f4f42efa3524
date added to LUP
2016-10-10 11:47:41
date last changed
2017-07-23 05:18:47
@article{8fd42bec-a38c-4059-a526-f4f42efa3524,
  abstract     = {<p>The activity and adsorption of three variants of human carbonic anhydrase (HCA) with similar topology but variation in charge and stability were studied in the presence of carboxyl-modified polystyrene nanoparticles of different sizes ranging from 25 nm to 114 nm. The balance of forces driving the adsorption of carbonic anhydrase variants is affected by the physicochemical properties of the protein and the nanoparticle size. All enzymes are totally inhibited upon adsorption due to the transition towards a molten globule like state that lacks enzymatic activity. The size of the particle affects the adsorption of human carbonic anhydrase I and N-terminal truncated human carbonic anhydrase II. Investigations on pH effects indicate that the size of the particle modulates the lateral interactions at the protein layer for these particular variants whose adsorption is mainly driven by electrostatic forces. A third variant, human carbonic anhydrase II, instead shows no strong influence of nanoparticle size which supports an adsorption process mainly driven by the hydrophobic effect.</p>},
  author       = {Assarsson, A. and Nasir, I. and Lundqvist, M. and Cabaleiro-Lago, C.},
  issn         = {2046-2069},
  language     = {eng},
  number       = {42},
  pages        = {35868--35874},
  publisher    = {Royal Society of Chemistry},
  series       = {RSC Advances},
  title        = {Kinetic and thermodynamic study of the interactions between human carbonic anhydrase variants and polystyrene nanoparticles of different size},
  url          = {http://dx.doi.org/10.1039/c6ra06175c},
  volume       = {6},
  year         = {2016},
}