Proteolytic cleavage reveals interaction patterns between silica nanoparticles and two variants of human carbonic anhydrase

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...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 21(2005), 25 vom: 06. Dez., Seite 11903-6
1. Verfasser: Lundqvist, Martin (VerfasserIn)
Weitere Verfasser: Andresen, Cecilia, Christensson, Sara, Johansson, Sara, Karlsson, Martin, Broo, Klas, Jonsson, Bengt-Harald
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Peptide Fragments Silicon Dioxide 7631-86-9 Carbonic Anhydrases EC 4.2.1.1
Beschreibung
Zusammenfassung: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
Beschreibung:Date Completed 23.04.2016
Date Revised 03.12.2018
published: Print
Citation Status MEDLINE
ISSN:1520-5827