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Protein Assembly Through Site-specific Interactions with Gold Nanoparticles

Published online by Cambridge University Press:  01 February 2011

Minghui Hu,
Luping Qian,
Raymond P Briñas,
Elena S Lymar and
James F Hainfeld
Minghui Hu
Affiliation:
mhu@bnl.gov, Brookhaven National Laboratory, Biology Department, Brookhaven National Laboratory, Upton, NY, 11973, United States, 631 344 3747, 631 344 3407
Luping Qian
Affiliation:
lqian@bnl.gov, Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
Raymond P Briñas
Affiliation:
rbrinas@bnl.gov, Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
Elena S Lymar
Affiliation:
lymare@bnl.gov, Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
James F Hainfeld
Affiliation:
hainfeld@bnl.gov, Brookhaven National Laboratory, Biology Department, Upton, NY, 11973, United States
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Abstract

A universal method is described to design and construct protein-nanoparticle assemblies controlled by nanoparticle functionality, and placement of genetic tag into proteins. Well-defined binding complexes of nanoparticles and two proteins, the adenovirus serotype 12 knob and the mycobacterium tuberculosis 20S proteasome, were formed through site-specific binding between 6x-histidine tags in proteins and nickel-nitrilotriacetic acid functional groups on gold nanoparticles.

Keywords

nanostructurebiological synthesis (assembly)transmission electron microscopy (TEM)

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References

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