Protein−Nanoparticle Interaction: Identification of the Ubiquitin−Gold Nanoparticle Interaction Site

Calzolai, Luigi; Franchini, Fabio; Gilliland, Douglas; Rossi, François

doi:10.1021/nl101746v

Cited by 243 publications

(270 citation statements)

References 24 publications

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“…However, aggregation can be avoided if sufficient BSA is added to PBS. This may be attributed to the following reasons: firstly, BSA forms a protective layer on the AuNPs surface, and the colloidal suspensions could be stabilized by the interaction of protein side chains or domains, resulting in a reduction in entropy and a loss of solvation enthalpy, both of which keep the system stable [29]; secondly, BSA bound to the AuNPs surface is continuously exchanged with free BSA [20], which should also improve the stability of the AuNPs solution. Because AuNPs started to aggregate when the BSA concentration decreased to below 30 nmol/L, this roughly indicates the critical concentration of BSA to prevent AuNP aggregation.…”

Section: Effect Of Bsa Concentration On the Aunps Stabilitymentioning

confidence: 99%

“…Some studies have investigated the influence of AuNP size on the conformation of cytochrome c [14]; and the effect of pH on the conformation of BSA adsorbed on the surface of AuNPs [15]. Fluorescence spectroscopy [11,16], dynamic light scattering [8,17], circular dichroism [9,18], Fourier transform infrared spectroscopy (FTIR) [19], nuclear magnetic resonance spectroscopy [20], surface enhanced Raman scattering [21], time-correlated single photon counting spectroscopy [13,22] are among a variety of techniques commonly used to characterize AuNPs-protein interactions. The combination of different techniques will give us insight into the interactions of AuNPs and proteins.…”

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confidence: 99%

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Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Shi

Xie

et al. 2012

Chin. Sci. Bull.

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The interactions between bovine serum albumin (BSA) and gold nanoparticles (AuNPs), and the conformational changes of BSA induced by this interaction, were investigated by UV-visible absorption spectroscopy, fluorescence spectroscopy, and Fourier transform infrared in combination with attenuated total reflection spectroscopy (ATR-FTIR). The critical adsorption density for preventing AuNP aggregation in 0.1 mol/L phosphate buffered saline (pH 7.2) was 23 BSA molecules per gold particle or 3.8×1012 BSA molecules/cm 2 . BSA bound to the AuNPs with high affinity (binding constant K s =7.59×10 8 L/mol), and the intrinsic fluorescence of BSA was quenched by the AuNPs in accordance with the static quenching mechanism. Both fluorescence spectroscopy and ATR-FTIR showed that AuNPs induced conformational changes in BSA, which resulted in it becoming less compact and increased the polarity of the microenvironment around the tryptophan residue Trp-212.

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Section: Effect Of Bsa Concentration On the Aunps Stabilitymentioning

confidence: 99%

mentioning

confidence: 99%

Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Shi

Xie

et al. 2012

Chin. Sci. Bull.

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“…This means that a sufficiently close approach by the AF488 acceptor to the donor may be disfavored due to hindrance by the specific, and perhaps non-random, orientation of anti-OA antibody-F ab complex with respect to LaNP as has been noted for other systems. 28 Further confirmation of resonance energy transfer within the system was obtained through photoluminescence lifetime measurements which, using a longer gated delay of 500 µs, avoids interference from direct excitation of the AF488 acceptor. For excitation at 266 nm, data showed a mono-exponential decay more than 13% faster for the LaNP-OA-anti-OA antibody-AF488 complex (1.91 ms) compared to the LaNP only (2.20 ms) indicating increased de-excitation efficiency based on energy transfer to the short fluorescence lifetime acceptor.…”

Section: Resultsmentioning

confidence: 99%

Application of Functionalized Lanthanide-Based Nanoparticles for the Detection of Okadaic Acid-Specific Immunoglobulin G

Stipić

Pletikapić²,

Jakšić

et al. 2015

J. Phys. Chem. B

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Marine biotoxins are widespread in the environment and impact on human health via contaminated shellfish, causing diarrhetic, amnesic, paralytic or neurotoxic poisoning. In spite of this methods for determining if poisoning has occurred are limited. We show the development of a simple and sensitive luminescence resonance energy transfer (LRET) -based concept which allows the detection of anti-okadaic acid rabbit polyclonal IgG (mouse monoclonal IgG1) using functionalized lanthanide-based nanoparticles. Upon UV excitation, the functionalized nanoparticles were shown to undergo LRET with fluorophore-labeled anti-okadaic acid antibodies which had been captured and bound by okadaic acid-decorated nanoparticles. The linear dependence of fluorescence emission intensity with antigen-antibody binding events was recorded in the nanomolar to micromolar range, while essentially no LRET signal was detected in the absence of antibody. These results may find applications in new, cheap and robust sensors for detecting not only immune responses to biotoxins but to a wide range of biomolecules based on antigen-antibody recognition systems. Further, as the system is based on solution chemistry it may be sufficiently simple and versatile to be applied at point-of-care.

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“…46 Molecular binding of an antibody to the surface of a gold nanoparticle is transduced to a colorimetric signal due to the changes in surface plasmon absorbance of the parent gold particle. Eventually, binding at the surface of functionalized gold particles results in a shift in peak wavelength as well as an increase in intensity ( Figure 10A).…”

Section: Discussionmentioning

confidence: 99%

Fungus-mediated biological synthesis of gold nanoparticles: potential in detection of liver cancer

Chauhan

Zubair²,

Tufail³

et al. 2011

IJN

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Background: Nanomaterials are considered to be the pre-eminent component of the rapidly advancing field of nanotechnology. However, developments in the biologically inspired synthesis of nanoparticles are still in their infancy and consequently attracting the attention of material scientists throughout the world. Keeping in mind the fact that microorganism-assisted synthesis of nanoparticles is a safe and economically viable prospect, in the current study we report Candida albicans-mediated biological synthesis of gold nanoparticles. Methods and results: Transmission electron microscopy, atomic force microscopy, and various spectrophotometric analyses were performed to characterize the gold nanoparticles. The morphology of the synthesized gold particles depended on the abundance of C. albicans cytosolic extract. Transmission electron microscopy, nanophox particle analysis, and atomic force microscopy revealed the size of spherical gold nanoparticles to be in the range of 20-40 nm and nonspherical gold particles were found to be 60-80 nm. We also evaluated the potential of biogenic gold nanoparticles to probe liver cancer cells by conjugating them with liver cancer cell surface-specific antibodies. The antibody-conjugated gold particles were found to bind specifically to the surface antigens of the cancer cells. Conclusion:The antibody-conjugated gold particles synthesized in this study could successfully differentiate normal cell populations from cancerous cells.

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Protein−Nanoparticle Interaction: Identification of the Ubiquitin−Gold Nanoparticle Interaction Site

Cited by 243 publications

References 24 publications

Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Application of Functionalized Lanthanide-Based Nanoparticles for the Detection of Okadaic Acid-Specific Immunoglobulin G

Fungus-mediated biological synthesis of gold nanoparticles: potential in detection of liver cancer

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