Control of Protein Structure and Function through Surface Recognition by Tailored Nanoparticle Scaffolds

Hong, Rui; Fischer, Nicholas O.; Verma, Ayush; Goodman, Catherine; Emrick, Todd; Rotello, Vincent M.

doi:10.1021/ja037470o

Cited by 280 publications

(238 citation statements)

References 31 publications

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“…Relying on the resistance of OEG to nonspecific interactions with biomolecules, [24] tetra(ethylene glycol) spacers were introduced at the nanoparticle-protein interface. [25] Structural data obtained from fluorescence and circular dichroism (CD) studies revealed that the nanoparticle-bound ChT remained with native structure. Further studies demonstrated that nanoparticle-protein complexation can considerably stabilize the bound proteins against denaturation at the air/water interface.…”

Section: Review Articlementioning

confidence: 99%

Applications of Nanoparticles in Biology

2008

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Section: Review Articlementioning

confidence: 99%

Applications of Nanoparticles in Biology

2008

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“…This problem could cause uncertainty in the quantitative analysis. In addition to fluorescence, circular dichroism [22,25,26] and FT-IR spectroscopy [22] are often used to monitor protein conformation change upon binding with gold nanoparticles. Calzolai et al identified ubiquitin-gold nanoparticle interaction site using NMR spectroscopy [27].…”

Section: Introductionmentioning

confidence: 99%

Dynamic light scattering for gold nanorod size characterization and study of nanorod–protein interactions

2012

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In recent years, there has been considerable interest and research activity in using gold nanoparticle materials for biomedical applications including biomolecular detection, bioimaging, drug delivery, and photothermal therapy. In order to apply gold nanoparticles in the real biological world, we need to have a better understanding of the potential interactions between gold nanoparticle materials and biomolecules in vivo and in vitro. Here, we report the use of dynamic light scattering (DLS) for gold nanorods characterization and nanorod-protein interaction study. In the size distribution diagram, gold nanorods with certain aspect ratios exhibit two size distribution peaks, one with an average hydrodynamic diameter at 5-7 nm, and one at 70-80 nm. The small size peak is attributed to the rotational diffusion of the nanorods instead of an actual dimension of the nanorods. When proteins are adsorbed to the gold nanorods, the average particle size of the nanorods increases and the rotational diffusion-related size distribution peak also changes dramatically. We examined the interaction between four different proteins, bovine serum albumin, human serum albumin, immunoglobulin G, and immunoglobulin A (IgA) with four gold nanorods that have the same diameter but different aspect ratios. From this study, we found that protein adsorption to gold nanorods is strongly dependent on the aspect ratio of the nanorods, and varies significantly from protein to protein. The two serum albumin proteins caused nanorod aggregation upon interaction with the nanorods, while the two immunoglobulin proteins formed a stable protein corona on the nanorod surface without causing significant nanorod aggregation. This study demonstrates that DLS is a valuable tool for nanorod characterization. It reveals information complementary to molecular spectroscopic techniques on gold nanorod-protein interactions.

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“…The prediction was also confirmed by comparing the results of gel electrophoresis. Furthermore, gel electrophoresis has been previously utilised in nanotechnology to investigate the biding behaviour of L-lysine [24], to separate DNA-capped nanogold [25,26] and protein-capped GNPs [27].…”

Section: Introductionmentioning

confidence: 99%

Fabrication of capped gold nanoparticles by using various amino acids

Zare

Khoshnevisan

Barkhi

et al. 2013

Journal of Experimental Nanoscience

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The production of gold nanoparticles (GNPs) by amino acid is one of the most attractive and interesting subjects in nanobiotechnology. In this study, amino acids have been utilised as a reducing agent and also an agent for capping GNPs. The GNPs were prepared using a reduction solution containing gold cations with optimum concentration of gold salt (5 mM), and also functionalised by glutamic acid, phenylalanine and tryptophan with optimum concentration of amino acids (25 mM). The optimum condition of gold solution and amino acids were achieved by ultraviolet-visible spectroscopy. The size of nanoparticles was obtained 5-20, 10-20 and 20-30 nm, respectively, by transmission electron microscopy and dynamic light scattering techniques. The results obtained from experimental and quantum calculations confirm that amino acids have strong bond while they have anion binding. Moreover, the free carboxylic groups of capped GNPs are one of the suitable and capable beads for binding biological agents. As a result, the medical applications of amino acids and proteins can be used as a practical method due to the strong interaction of peripheral amine groups with nanoparticles.

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Control of Protein Structure and Function through Surface Recognition by Tailored Nanoparticle Scaffolds

Cited by 280 publications

References 31 publications

Applications of Nanoparticles in Biology

Applications of Nanoparticles in Biology

Dynamic light scattering for gold nanorod size characterization and study of nanorod–protein interactions

Fabrication of capped gold nanoparticles by using various amino acids

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