Anomalous adsorptive properties of HIV protease: indication of two-dimensional crystallization?
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18304786
DOI
10.1016/j.colsurfb.2008.01.011
PII: S0927-7765(08)00029-5
Knihovny.cz E-zdroje
- MeSH
- adsorpce MeSH
- HIV-proteasa chemie farmakokinetika MeSH
- HIV chemie enzymologie MeSH
- krystalizace MeSH
- lidé MeSH
- povrchová plasmonová rezonance MeSH
- povrchové vlastnosti MeSH
- termodynamika MeSH
- zlato MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- HIV-proteasa MeSH
- zlato 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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