Effect of Protein Adsorption on the Fluorescence of Ultrasmall Gold Nanoclusters

Li, Shang; Brandholt, Stefan; Stockmar, Florian; Trouillet, Vanessa; Bruns, Michael; Nienhaus, G. Ulrich

doi:10.1002/smll.201101353

Cited by 163 publications

(147 citation statements)

References 43 publications

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“…2,3,15,17,22 Luminescence of Au 25 NCs was observed by many groups, and different fluorescent wavelengths were found for Au 25 NCs protected by different ligands between 640 and 750 nm, such as BSA at 640 nm 22 and 674 nm, 47 phenyl ethane thiol at 750 nm, 3 glutathione at 700 nm, 15 MSA at 700 nm, 17 pepsin at 670 nm, 48 and DHLA at 684 nm. 49 According to Zhu's calculations, thiol-protected Au 25 NCs have a HOMO−LUMO gap at 1.37 eV. 8 Therefore, the red band cannot originate from the transition of LUMO to HOMO.…”

Section: Resultsmentioning

confidence: 99%

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters

et al. 2012

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In this work, we investigated the temperature-dependent luminescence of bovine serum albumin-protected Au 25 nanoclusters and the correlation with their structure. Our experiments reveal that the red luminescence consists of two bands, namely, band I at 710 nm and band II at 640 nm. The temperature dependence of band I exhibits similarity to semiconductors, such as a red shift of emission and bandwidth broadening upon increasing temperatures due to electron−phonon and electron−defect/surface scattering. In contrast, band II exhibits different temperature dependence. It is concluded that band I exclusively originates from the icosahedral core of 13 Au(0) atoms and band II dominantly arises from the [−S−Au(I)−S−Au(I)−S−] staples. Moreover, with increasing temperatures, the intensity of band I and band II decreases. A similar activation energy was extracted, which is attributed to thermally activated defect/surface trapping. In addition, the relaxation from band II to band I was found to be inactive from 300 K down to 77 K.

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Section: Resultsmentioning

confidence: 99%

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters

et al. 2012

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“…To quantify the NP−protein interaction and to allow comparisons between information derived by different experimental approaches, apparent binding affinities can be determined as previously described using CD spectroscopy, 7 fluorescence spectroscopy, 53 and fluorescence correlation spectroscopy (FCS). 36,48 It should be noted that CD measurements will generally refer to the so-called "hard" corona.…”

Section: Resultsmentioning

confidence: 99%

Impact of the Nanoparticle–Protein Corona on Colloidal Stability and Protein Structure

et al. 2012

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In biological fluids, proteins may associate with nanoparticles (NPs), leading to the formation of a so-called "protein corona" largely defining the biological identity of the particle. Here, we present a novel approach to assess apparent binding affinities for the adsorption/desorption of proteins to silver NPs based on the impact of the corona formation on the agglomeration kinetics of the colloid. Affinities derived from circular dichroism measurements complement these results, simultaneously elucidating structural changes in the adsorbed protein. Employing human serum albumin as a model, apparent affinities in the nanomolar regime resulted from both approaches. Collectively, our findings now allow discrimination between the formation of protein mono- and multilayers on NP surfaces.

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“…A layer of proteins forms on the NP surfaces, the so-called protein corona [10,[31][32][33][34][35][36][37][38][39][40][41][42][43]. Consequently, cell surface receptors, which activate the endocytosis machinery, actually encounter NPs enshrouded in biomolecules rather than bare particles.…”

Section: Introductionmentioning

confidence: 99%

New views on cellular uptake and trafficking of manufactured nanoparticles

Treuel

Jiang

Nienhaus

2013

J. R. Soc. Interface.

315

224

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Nanoparticles (NPs) are of similar size to typical cellular components and proteins, and can efficiently intrude living cells. A detailed understanding of the involved processes at the molecular level is important for developing NPs designed for selective uptake by specific cells, for example, for targeted drug delivery. In addition, this knowledge can greatly assist in the engineering of NPs that should not penetrate cells so as to avoid adverse health effects. In recent years, a wide variety of experiments have been performed to elucidate the mechanisms underlying cellular NP uptake. Here, we review some select recent studies, which are often based on fluorescence microscopy and sophisticated strategies for specific labelling of key cellular components. We address the role of the protein corona forming around NPs in biological environments, and describe recent work revealing active endocytosis mechanisms and pathways involved in their cellular uptake. Passive uptake is also discussed. The current state of knowledge is summarized, and we point to issues that still need to be addressed to further advance our understanding of cellular NP uptake.

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Effect of Protein Adsorption on the Fluorescence of Ultrasmall Gold Nanoclusters

Cited by 163 publications

References 43 publications

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters

Impact of the Nanoparticle–Protein Corona on Colloidal Stability and Protein Structure

New views on cellular uptake and trafficking of manufactured nanoparticles

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Effect of Protein Adsorption on the Fluorescence of Ultrasmall Gold Nanoclusters

Cited by 163 publications

References 43 publications

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au25 Nanoclusters

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au25 Nanoclusters

Impact of the Nanoparticle–Protein Corona on Colloidal Stability and Protein Structure

New views on cellular uptake and trafficking of manufactured nanoparticles

Contact Info

Product

Resources

About

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters

Structure-Correlated Dual Fluorescent Bands in BSA-Protected Au₂₅ Nanoclusters