The effect of nanoparticles on the structure and enzymatic activity of human carbonic anhydrase I and II
(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)
- author
- Cabaleiro-Lago, Celia LU and Lundqvist, Martin LU
- organization
- publishing date
- 2020-10
- 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
- MDPI AG
- external identifiers
-
- pmid:32992797
- scopus:85092053622
- 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
- 2024-04-03 14:16:06
@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}},
keywords = {{Human carbonic anhydrase; Interaction; Kinetics; Nanoparticles; Structure}},
language = {{eng}},
number = {{19}},
publisher = {{MDPI AG}},
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}},
}