Advanced

The effect of nanoparticles on the structure and enzymatic activity of human carbonic anhydrase I and II

Cabaleiro-Lago, Celia LU and Lundqvist, Martin LU (2020) In Molecules 25(19).
Abstract

Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to... (More)

Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to alteration of the original function of the protein. However, if the function is preserved interesting biotechnological applications can be developed. This review will cover the knowledge about the interaction between hCAs and nanomaterials. We will highlight how the interaction may lead to conformational changes that render the enzyme inactive. Moreover, the importance of different factors on the final effect on hCAs, such as protein stability, protein hydrophobic or charged patches and chemistry of the nanoparticle surface will be discussed.

(Less)
Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Human carbonic anhydrase, Interaction, Kinetics, Nanoparticles, Structure
in
Molecules
volume
25
issue
19
article number
4405
publisher
Molecular Diversity Preservation International
external identifiers
  • scopus:85092053622
  • pmid:32992797
ISSN
1420-3049
DOI
10.3390/molecules25194405
language
English
LU publication?
yes
id
d45f622e-ce50-429c-96a2-ce1691586dab
date added to LUP
2020-11-02 15:05:42
date last changed
2021-01-06 03:35:37
@article{d45f622e-ce50-429c-96a2-ce1691586dab,
  abstract     = {<p>Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to alteration of the original function of the protein. However, if the function is preserved interesting biotechnological applications can be developed. This review will cover the knowledge about the interaction between hCAs and nanomaterials. We will highlight how the interaction may lead to conformational changes that render the enzyme inactive. Moreover, the importance of different factors on the final effect on hCAs, such as protein stability, protein hydrophobic or charged patches and chemistry of the nanoparticle surface will be discussed.</p>},
  author       = {Cabaleiro-Lago, Celia and Lundqvist, Martin},
  issn         = {1420-3049},
  language     = {eng},
  number       = {19},
  publisher    = {Molecular Diversity Preservation International},
  series       = {Molecules},
  title        = {The effect of nanoparticles on the structure and enzymatic activity of human carbonic anhydrase I and II},
  url          = {http://dx.doi.org/10.3390/molecules25194405},
  doi          = {10.3390/molecules25194405},
  volume       = {25},
  year         = {2020},
}