Abstract
Human rhinovirus serotype 2 (HRV2) specifically binds to very-low-density lipoprotein receptor
(VLDLR). Among the eight extracellular repeats of VLDLR, the third module (V3) has the highest affinity
for the virus, and 12 copies of the genetically engineered concatamer V33333-His6 were found to bind per
virus particle. In the present study, ring formation of V33333-His6 about each of the 12 5-fold symmetry
axes on HRV2 was demonstrated by fluorescence resonance energy transfer (FRET) between donor and
acceptor on N- and C-terminus, respectively. In particular, the N-terminus of V33333-His6 was labeled with
fluorescein, and the C-terminus with a new quencher which was bound to the His6 tag with nanomolar
affinity (Kd ∼10-8 M) in the presence of 2 μM NiCl2.
| Original language | English |
|---|---|
| Pages (from-to) | 5478 |
| Number of pages | 5 |
| Journal | Journal of the American Chemical Society |
| Volume | 131 |
| Publication status | Published - 2009 |
Fields of science
- 103 Physics, Astronomy
- 104003 Inorganic chemistry
- 204 Chemical Process Engineering
- 104016 Photochemistry
- 104021 Structural chemistry
- 106032 Photobiology
- 106002 Biochemistry
- 210006 Nanotechnology
- 107 Other Natural Sciences
- 211908 Energy research
- 301904 Cancer research
- 301305 Medical chemistry
- 105904 Environmental research
JKU Focus areas
- Nano-, Bio- and Polymer-Systems: From Structure to Function
- Engineering and Natural Sciences (in general)
