Protein Assembly Through Site-specific Interactions with Gold Nanoparticles

2006 ◽  
Vol 951 ◽  
Author(s):  
Minghui Hu ◽  
Luping Qian ◽  
Raymond P Briñas ◽  
Elena S Lymar ◽  
James F Hainfeld
Keyword(s):  
Gold Nanoparticles ◽  
Specific Binding ◽  
Nitrilotriacetic Acid ◽  
Protein Assembly ◽  
20S Proteasome ◽  
Universal Method ◽  
Specific Interactions ◽  
Adenovirus Serotype ◽  
Site Specific ◽  
Nanoparticle Assemblies

ABSTRACTA 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.

scholarly journals DNA-mediated self-assembly of gold nanoparticles on protein superhelix

2018 ◽  
Author(s):  
Tao Zhang ◽  
Ingemar André
Keyword(s):  
Gold Nanoparticles ◽  
Self Assembly ◽  
De Novo ◽  
Specific Binding ◽  
Protein Structures ◽  
Spatial Arrangement ◽  
Inorganic Nanoparticles ◽  
Covalent Attachment ◽  
Site Specific ◽  
Conjugation Method

AbstractRecent advances in protein engineering have enabled methods to control the self-assembly of protein on various length-scales. One attractive application for designed proteins is to direct the spatial arrangement of nanomaterials of interest. Until now, however, a reliable conjugation method is missing to facilitate site-specific positioning. In particular, bare inorganic nanoparticles tend to aggregate in the presence of buffer conditions that are often required for the formation of stable proteins. Here, we demonstrated a DNA mediated conjugation method to link gold nanoparticles with protein structures. To achieve this, we constructed de novo designed protein fibers based on previously published uniform alpha-helical units. DNA modification rendered gold nanoparticles with increased stability against ionic solutions and the use of complementary strands hybridization guaranteed the site-specific binding to the protein. The combination of high resolution placement of anchor points in designed protein assemblies with the increased control of covalent attachment through DNA binding can enable investigations of multilevel physical coupling events of nanocomponents on protein templates and expand the application of protein structures to material sciences.

An antibody-based amperometric biosensor for 20S proteasome activity and inhibitor screening

The Analyst ◽  
2021 ◽  
Author(s):  
Madalina M. Barsan ◽  
Victor C. Diculescu
Keyword(s):  
Proteasome Activity ◽  
Electrochemical Methods ◽  
Amperometric Biosensor ◽  
20S Proteasome ◽  
Specific Interactions ◽  
Inhibitor Screening

The 20S proteasome is immobilized through specific interactions with antibodies and its activity is evaluated by electrochemical methods.

scholarly journals Site-Specific Binding of Non-Site-Specific Ions

2019 ◽  
Vol 116 (12) ◽  
pp. 2237-2239 ◽  
Author(s):  
Shi-Jie Chen
Keyword(s):  
Specific Binding ◽  
Site Specific

Molecular modulation of calcium oxalate crystallization

2006 ◽  
Vol 291 (6) ◽  
pp. F1123-F1132 ◽  
Author(s):  
James J. De Yoreo ◽  
S. Roger Qiu ◽  
John R. Hoyer
Keyword(s):  
Molecular Modeling ◽  
Calcium Oxalate ◽  
Stone Formation ◽  
Energy Levels ◽  
Critical Role ◽  
Specific Interactions ◽  
Crystal Surfaces ◽  
Site Specific

Calcium oxalate monohydrate (COM) is the primary constituent of the majority of renal stones. Osteopontin (OPN), an aspartic acid-rich urinary protein, and citrate, a much smaller molecule, are potent inhibitors of COM crystallization at levels present in normal urine. Current concepts of the role of site-specific interactions in crystallization derived from studies of biomineralization are reviewed to provide a context for understanding modulation of COM growth at a molecular level. Results from in situ atomic force microscopy (AFM) analyses of the effects of citrate and OPN on growth verified the critical role of site-specific interactions between these growth modulators and individual steps on COM crystal surfaces. Molecular modeling investigations of interactions of citrate with steps and faces on COM crystal surfaces provided links between the stereochemistry of interaction and the binding energy levels that underlie mechanisms of growth modification and changes in overall crystal morphology. The combination of in situ AFM and molecular modeling provides new knowledge that will aid rationale design of therapeutic agents for inhibition of stone formation.

scholarly journals Site-specific binding of wild-type p53 to cellular DNA is inhibited by SV40 T antigen and mutant p53.

1992 ◽  
Vol 6 (10) ◽  
pp. 1886-1898 ◽  
Author(s):  
J Bargonetti ◽  
I Reynisdottir ◽  
P N Friedman ◽  
C Prives
Keyword(s):  
Specific Binding ◽  
T Antigen ◽  
Mutant P53 ◽  
Wild Type ◽  
Sv40 T Antigen ◽  
Site Specific ◽  
Wild Type P53 ◽  
Cellular Dna

Site-specific interactions of copper(II) ions with heparin revealed with complementary (SRCD, NMR, FTIR and EPR) spectroscopic techniques

2008 ◽  
Vol 343 (12) ◽  
pp. 2184-2193 ◽  
Author(s):  
T.R. Rudd ◽  
M.A. Skidmore ◽  
S.E. Guimond ◽  
M. Guerrini ◽  
C. Cosentino ◽  
...  
Keyword(s):  
Spectroscopic Techniques ◽  
Specific Interactions ◽  
Site Specific
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