Assembly of Nanoparticle–Protein Binding Complexes: From Monomers to Ordered Arrays

Hu, Minghui; Qian, Luping; Briñas, Raymond P.; Lymar, Elena S.; Hainfeld, James F.

doi:10.1002/ange.200701180

Cited by 17 publications

(16 citation statements)

References 39 publications

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“…1). Our previous results showed that the proteasomes were assembled into 2D arrays with a 1:1 stoichiometry between Au NP and proteasome when incubated with Ni-NTA Au NPs (Hu et al, 2007). In this study, image analysis showed that averaged top-view images from the proteasome arrays gave more accurate structural information at a higher resolution using fewer protein particles than those from the single particles without Au NPs.…”

Section: Introductionmentioning

confidence: 62%

“…Ni-NTA functionalized Au NPs were synthesized following our published method (Hu et al, 2007). In brief, hydrogen tetrachloroaurate (HAuCl 4 ) was reduced using sodium borohydride (NaBH 4 ) in the presence of L-glutathione (c-glu-cys-gly, GSH) and (1S)-N-[5-[(4-mercaptobutanoyl)amino]-1-carboxypentyl]iminodiacetic (Lys-NTA-SH) at pH 7.0, followed by treatment with a solution of NiCl 2 to convert Au NPs into Ni-NTA Au NPs.…”

Section: Synthesis Of Ni-nta Au Nps and Assembly Of Mtb 20s Proteasomesmentioning

confidence: 99%

“…A 5-lL (4.3 mg/mL, 0.028 nmol) proteasome solution in 10 mM phosphate buffered saline (PBS, containing 150 mM NaCl) at pH 7.5 was added to a 30-lL (0.17 mg/mL, 0.014 nmol) aqueous solution of 3.9-nm Ni-NTA Au NPs, followed by incubation at 4°C for 2-3 days (Hu et al, 2007). This solution was used for TEM and other analyses.…”

Section: Synthesis Of Ni-nta Au Nps and Assembly Of Mtb 20s Proteasomesmentioning

confidence: 99%

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Gold nanoparticle–protein arrays improve resolution for cryo-electron microscopy

Qian

Briñas

et al. 2008

Journal of Structural Biology

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Cryo-electron microscopy single particle analysis shows limited resolution due to poor alignment precision of noisy images taken under low electron exposure. Certain advantages can be obtained by assembling proteins into two-dimensional (2D) arrays since protein particles are locked into repetitive orientation, thus improving alignment precision. We present a labeling method to prepare protein 2D arrays using gold nanoparticles (NPs) interconnecting genetic tag sites on proteins. As an example, mycobacterium tuberculosis 20S proteasomes tagged with 6x-histidine were assembled into 2D arrays using 3.9-nm Au NPs functionalized with nickel-nitrilotriacetic acid. The averaged top-view images from the array particles showed higher resolution (by 6-8A) compared to analysis of single particles. The correct 7-fold symmetry was also evident by using array particles whereas it was not clear by analysis of a comparable number of single particles. The applicability of this labeling method for three-dimensional reconstruction of biological macromolecules is discussed.

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Section: Introductionmentioning

confidence: 62%

Section: Synthesis Of Ni-nta Au Nps and Assembly Of Mtb 20s Proteasomesmentioning

confidence: 99%

Section: Synthesis Of Ni-nta Au Nps and Assembly Of Mtb 20s Proteasomesmentioning

confidence: 99%

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Gold nanoparticle–protein arrays improve resolution for cryo-electron microscopy

Qian

Briñas

et al. 2008

Journal of Structural Biology

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“…Currently, several types of Au-NPs have been developed as labeling reagents for transmission electron microscopy (TEM) analysis of proteins. 8,[17][18][19][20][21][22][23][24][25][26] However, many of these do not meet our requirements for single protein TEM analysis. Desirable Au-NPs should be water soluble, stable in aqueous solution without forming a precipitate and have a modest diameter of 2-5 nm.…”

Section: Resultsmentioning

confidence: 99%

“…This is because a large number of NTA moieties per one gold particle lead to the assembly of proteins on the Au-NP through multiple crosslinking reactions. 24 Furthermore, because of the small size (1.4 or 1.8 nn on average), it is difficult to detect all Au-NPs directly in a TEM image.…”

Section: Resultsmentioning

confidence: 99%

Electron Microscopic Visualization of the Filament Binding Mode of Actin-Binding Proteins

Ito

Hirayama

Taki

et al. 2011

Journal of Molecular Biology

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One‐Dimensional Gold Nanoparticle Arrays by Electrostatically Directed Organization Using Polypeptide Self‐Assembly

et al. 2009

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The study of interactions between particles organized in a linear configuration is interesting from a quantum mechanical perspective, and the anisotropic properties of linear assemblies is of potential interest for the development of solid-state devices. [1][2][3] This anisotropy may be manifested as a difference in the magnetization and coercivity obtained in a magneticnanoparticle array when a field is applied along the chain or orthogonal to it. [4,5 ] Nonlinear electrical characteristics [3] or dichroism in the optical spectra with longitudinal and transverse polarizations of light [6,7 ] in metal nanoparticle arrays are other examples of such anisotropy, and the construction of such arrays would offer opportunities in multiple applications. Engineering matter at submicron length scales has been an area largely dominated by top-down methodologies. Control of interparticle spacing in metal-nanoparticle arrays by using techniques such as electron beam lithography has been found to have a dramatic impact on the optical response of the nanoparticle assembly, [8][9][10] ] and has implications in fields such as plasmonics [11] and energy transport. [12,13 ] The use of templates such as carbon nanotubes [14] and linear pores[15] to construct one-dimensional nanostructures has been demonstrated previously. In addition, polymers have recently begun to play an increasingly active role as elements that can reproducibly direct the arrangement of nanoparticles into functional geometries. [16,17 ] Self assembling systems offer convenient yet powerful bottom-up strategies for the creation of nanostructures that can be deployed in the realization of functional nanoscale devices. [18,19 ] The utilization of biomolecules such as DNA, [3, 20 -24 ] and protein-based materials [25][26][27] or viruses [28,29 ] to dictate the organization of nanoparticles has been shown to be an effective and robust paradigm. The use of peptide-based structures [30,31 ] in nanotechnology confers numerous advantages such as the specification of assembled nanostructure by changes in the primary sequence of the peptide, as well as the adoption of various hierarchical morphologies **

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Assembly of Nanoparticle–Protein Binding Complexes: From Monomers to Ordered Arrays

Cited by 17 publications

References 39 publications

Gold nanoparticle–protein arrays improve resolution for cryo-electron microscopy

Gold nanoparticle–protein arrays improve resolution for cryo-electron microscopy

Electron Microscopic Visualization of the Filament Binding Mode of Actin-Binding Proteins

One‐Dimensional Gold Nanoparticle Arrays by Electrostatically Directed Organization Using Polypeptide Self‐Assembly

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