Proteolytic cleavage reveals interaction patterns between silica nanoparticles and two variants of human carbonic anhydrase
(2005) In Langmuir 21(25). p.11903-11906- Abstract
- To characterize the sites on the protein surface that are involved in the adsorption to silica nanoparticles and the subsequent rearrangements of the protein/nanoparticle interaction, a novel approach has been used. After incubation of protein with silica nanoparticles for 2 or 16 h, the protein was cleaved with trypsin and the peptide fragments were analyzed with mass spectrometry. The nanoparticle surface area was in 16-fold excess over available protein surface to minimize the probability that the initial binding would be affected by other protein molecules. When the fragment patterns obtained in the presence and absence of silica nanoparticles were compared, we were able to characterize the protein fragments that interact with the... (More)
- To characterize the sites on the protein surface that are involved in the adsorption to silica nanoparticles and the subsequent rearrangements of the protein/nanoparticle interaction, a novel approach has been used. After incubation of protein with silica nanoparticles for 2 or 16 h, the protein was cleaved with trypsin and the peptide fragments were analyzed with mass spectrometry. The nanoparticle surface area was in 16-fold excess over available protein surface to minimize the probability that the initial binding would be affected by other protein molecules. When the fragment patterns obtained in the presence and absence of silica nanoparticles were compared, we were able to characterize the protein fragments that interact with the surface. This approach has allowed us to identify the initial binding sites on the protein structure and the rearrangement of the binding sites that occur upon prolonged incubation with the surface. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/6992617f-fa12-435d-90a1-7a1396a25aec
- author
- Lundqvist, Martin LU ; Andresen, Cecilia ; Christensson, Sara ; Johansson, Sara ; Karlsson, Martin ; Broo, Klas and Jonsson, Bengt-Harald
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 21
- issue
- 25
- pages
- 4 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:29444432262
- ISSN
- 0743-7463
- DOI
- 10.1021/la050477u
- language
- English
- LU publication?
- no
- id
- 6992617f-fa12-435d-90a1-7a1396a25aec
- date added to LUP
- 2021-10-19 12:00:27
- date last changed
- 2022-02-02 00:39:27
@article{6992617f-fa12-435d-90a1-7a1396a25aec,
abstract = {{To characterize the sites on the protein surface that are involved in the adsorption to silica nanoparticles and the subsequent rearrangements of the protein/nanoparticle interaction, a novel approach has been used. After incubation of protein with silica nanoparticles for 2 or 16 h, the protein was cleaved with trypsin and the peptide fragments were analyzed with mass spectrometry. The nanoparticle surface area was in 16-fold excess over available protein surface to minimize the probability that the initial binding would be affected by other protein molecules. When the fragment patterns obtained in the presence and absence of silica nanoparticles were compared, we were able to characterize the protein fragments that interact with the surface. This approach has allowed us to identify the initial binding sites on the protein structure and the rearrangement of the binding sites that occur upon prolonged incubation with the surface.}},
author = {{Lundqvist, Martin and Andresen, Cecilia and Christensson, Sara and Johansson, Sara and Karlsson, Martin and Broo, Klas and Jonsson, Bengt-Harald}},
issn = {{0743-7463}},
language = {{eng}},
number = {{25}},
pages = {{11903--11906}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Proteolytic cleavage reveals interaction patterns between silica nanoparticles and two variants of human carbonic anhydrase}},
url = {{http://dx.doi.org/10.1021/la050477u}},
doi = {{10.1021/la050477u}},
volume = {{21}},
year = {{2005}},
}