ArticleBiophysical journal2005
Protein adsorption orientation in the light of fluorescent probes: mapping of the interaction between site-directly labeled human carbonic anhydrase II and silica nanoparticles.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 58 citations in OpenAlex.
- Carbonic Anhydrase Robustness for Use in Nanoscale COACS omega · 2023Article
- The Effect of Nanoparticles on the Structure and Enzymatic Activity of Human Carbonic Anhydrase I and II.Molecules (Basel, Switzerland) · 2020Review
- Protein Interactions with Nanoparticle Surfaces: Highlighting Solution NMR Techniques.Israel journal of chemistry · 2019Article
- Immobilized carbonic anhydrase: preparation, characteristics and biotechnological applications.World journal of microbiology & biotechnology · 2018Review
- Article
- Chemical basis of interactions between engineered nanoparticles and biological systems.Chemical reviews · 2014Review
- Engineering lipid bilayer membranes for protein studies.International journal of molecular sciences · 2013Review
- Silica nanoconstruct cellular toleration threshold in vitro.Journal of controlled release : official journal of the Controlled Release Society · 2011Article
- Analytical strategies for detecting nanoparticle-protein interactions.The Analyst · 2010Review
- Differential modulation of the active site environment of human carbonic anhydrase XII by cationic quantum dots and polylysine.Biochimica et biophysica acta · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Little is known about the direction and specificity of protein adsorption to solid surfaces, a knowledge that is of great importance in many biotechnological applications. To resolve the direction in which a protein with known structure and surface potentials binds to negatively charged silica nanoparticles, fluorescent probes were attached to different areas on the surface of the protein human carbonic anhydrase II. By this approach it was clearly demonstrated that the adsorption of the native protein is specific to limited regions at the surface of the N-terminal domain of the protein. Furthermore, the adsorption direction is strongly pH-dependent. At pH 6.3, a histidine-rich area around position 10 is the dominating adsorption region. At higher pH values, when the histidines in this area are deprotonated, the protein is also adsorbed by a region close to position 37, which contains several lysines and arginines. Clearly the adsorption is directed by positively charged areas on the protein surface toward the negatively charged silica surface at conditions when specific binding occurs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.