Anomalous adsorptive properties of HIV protease: indication of two-dimensional crystallization?
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.
Cígler
Petr
P
Institute of Chemical Technology, Department of Analytical Chemistry, Technická 5, 166 28 Prague 6, Czech Republic.
Král
Vladimír
V
Kozísek
Milan
M
Konvalinka
Jan
J
Mirsky
Vladimir M
VM
D000327:Adsorption; D003460:Crystallization; D006046:Gold; D006678:HIV / Q000737:chemistry / Q000201:enzymology*; D016333:HIV Protease / Q000737:chemistry* / Q000493:pharmacokinetics*; D006801:Humans; D020349:Surface Plasmon Resonance; D013499:Surface Properties; D013816:Thermodynamics
D006046:Gold; D016333:HIV Protease