Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability
(2004) In Langmuir 20(24). p.10639-10647- Abstract
- We have analyzed the adsorption of protein to the surfaces of silica nanoparticles with diameters of 6, 9, and 15 nm. The effects upon adsorption on variants of human carbonic anhydrase with differing conformational stabilities have been monitored using methods that give complementary information, i.e., circular dichroism (CD), nuclear magnetic resonance (NMR), analytical ultracentrifugation (AUC), and gel permeation chromatography. Human carbonic anhydrase I (HCAI), which is the most stable of the protein variants, establishes a dynamic equilibrium between bound and unbound protein following mixture with silica particles. Gel permeation and AUC experiments indicate that the residence time of HCAI is on the order of ∼10 min and slowly... (More)
- We have analyzed the adsorption of protein to the surfaces of silica nanoparticles with diameters of 6, 9, and 15 nm. The effects upon adsorption on variants of human carbonic anhydrase with differing conformational stabilities have been monitored using methods that give complementary information, i.e., circular dichroism (CD), nuclear magnetic resonance (NMR), analytical ultracentrifugation (AUC), and gel permeation chromatography. Human carbonic anhydrase I (HCAI), which is the most stable of the protein variants, establishes a dynamic equilibrium between bound and unbound protein following mixture with silica particles. Gel permeation and AUC experiments indicate that the residence time of HCAI is on the order of ∼10 min and slowly increases with time, which allows us to study the effects of the interaction with the solid surface on the protein structure in more detail than would be possible for a process with faster kinetics. The effects on the protein conformation from the interaction have been characterized using CD and NMR measurements. This study shows that differences in particle curvature strongly influence the amount of the protein's secondary structure that is perturbed. Particles with a longer diameter allow formation of larger particle−protein interaction surfaces and cause larger perturbations of the protein's secondary structure upon interaction. In contrast, the effects on the tertiary structure seem to be independent of the particles' curvature. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5c2291c7-f030-4895-8578-405959809396
- author
- Lundqvist, Martin LU ; Sethson, Ingmar and Jonsson, Bengt-Harald
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 20
- issue
- 24
- pages
- 9 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:10044277018
- ISSN
- 0743-7463
- DOI
- 10.1021/la0484725
- language
- English
- LU publication?
- no
- id
- 5c2291c7-f030-4895-8578-405959809396
- date added to LUP
- 2021-10-19 11:49:57
- date last changed
- 2022-04-19 17:06:16
@article{5c2291c7-f030-4895-8578-405959809396,
abstract = {{We have analyzed the adsorption of protein to the surfaces of silica nanoparticles with diameters of 6, 9, and 15 nm. The effects upon adsorption on variants of human carbonic anhydrase with differing conformational stabilities have been monitored using methods that give complementary information, i.e., circular dichroism (CD), nuclear magnetic resonance (NMR), analytical ultracentrifugation (AUC), and gel permeation chromatography. Human carbonic anhydrase I (HCAI), which is the most stable of the protein variants, establishes a dynamic equilibrium between bound and unbound protein following mixture with silica particles. Gel permeation and AUC experiments indicate that the residence time of HCAI is on the order of ∼10 min and slowly increases with time, which allows us to study the effects of the interaction with the solid surface on the protein structure in more detail than would be possible for a process with faster kinetics. The effects on the protein conformation from the interaction have been characterized using CD and NMR measurements. This study shows that differences in particle curvature strongly influence the amount of the protein's secondary structure that is perturbed. Particles with a longer diameter allow formation of larger particle−protein interaction surfaces and cause larger perturbations of the protein's secondary structure upon interaction. In contrast, the effects on the tertiary structure seem to be independent of the particles' curvature.}},
author = {{Lundqvist, Martin and Sethson, Ingmar and Jonsson, Bengt-Harald}},
issn = {{0743-7463}},
language = {{eng}},
number = {{24}},
pages = {{10639--10647}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability}},
url = {{http://dx.doi.org/10.1021/la0484725}},
doi = {{10.1021/la0484725}},
volume = {{20}},
year = {{2004}},
}