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The utility of mutant VNPs displaying hexa-His tags as templates for
functionalization has also been shown. Mutant particles of P22, Ad, and
CPMV were successfully labeled with nanogold particles using Ni-NTA
linkers (Chatterji
, 2008). Besides
introducing functionalities using the His affinity tag, one can also make
use of the tag to achieve immobilization of the VNPs. This has been shown
for Q
et al.
, 2005; Kang
et al.
, 2008; Saini
et al.
b
and CPMV (Medintz
et al.
, 2005; Udit
et al.
, 2008).
Figure 4.17
Single M13 bacteriophage stretching and modification. (A) Rendering
of M13 bacteriophage stretching by an optical trap (not to scale). (B) The end
complexes of M13 (identified in purple) consist of several copies of genetically
modifiable pIX and pIII monomers, which have been modified with hexa-His
tags and biotin, respectively. (C) A transmission electron microscopic image
of the assembly architecture, where a gold-binding peptide was fused to pVIII
monomers (forms the virus body) for gold nanoparticle incorporation along the
length of the capsid. Reproduced with permission from Khalil, A. S., Ferrer, J. M.,
Brau, R. R., Kottmann, S. T., Noren, C. J., Lang, M. J., and Belcher, A. M. (2007) Single
M13 bacteriophage tethering and stretching,
Proc. Natl. Acad. Sci. USA,
104
(12),
4892-4897.
The biotin-streptavidin and hexa-His-Ni-NTA system can also be combined
on a single VNP. M13 particles, which display different proteins at each end
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