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.

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Author: Petr Cígler, Vladimír Král, Milan Kožíšek, Jan Konvalinka, Vladimir M. MirskyORCiDGND
DOI:https://doi.org/10.1016/j.colsurfb.2008.01.011
ISSN:0927-7765
Title of the source (English):Colloids and Surfaces B: Biointerfaces
Document Type:Scientific journal article peer-reviewed
Language:English
Year of publication:2008
Tag:HIV protease; Protein adsorption; Protein-resistant surfaces; Self-assembled monolayer; Surface plasmon resonance (SPR)
Volume/Year:64
Issue number:1
First Page:145
Last Page:149
Faculty/Chair:Fakultät 2 Umwelt und Naturwissenschaften / FG Nanobiotechnologie
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