Anomalous adsorptive properties of HIV protease: indication of two-dimensional crystallization?
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18304786
DOI
10.1016/j.colsurfb.2008.01.011
PII: S0927-7765(08)00029-5
Knihovny.cz E-resources
- MeSH
- Adsorption MeSH
- HIV Protease chemistry pharmacokinetics MeSH
- HIV chemistry enzymology MeSH
- Crystallization MeSH
- Humans MeSH
- Surface Plasmon Resonance MeSH
- Surface Properties MeSH
- Thermodynamics MeSH
- Gold MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- HIV Protease MeSH
- Gold MeSH
Adsorption of HIV protease onto surfaces that are usually considered to be protein-resistant was studied quantitatively using surface plasmon resonance. Adsorption onto gold surfaces functionalized by OH-terminated alkyl chains was much stronger than onto oligo(ethylene glycol)-terminated surfaces. Equilibrium and kinetic adsorption constants were determined. An anomalous mutual attraction between adsorbate molecules was observed, indicating the possibility of two-dimensional crystallization of HIV protease. These results are applicable for the design of sensors/biosensors for HIV protease resistance detection and for proper manipulation of this enzyme in laboratory devices.
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