Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Qu, Shaojian; Qiao, Zihan; Zhong, Wencheng; Liang, Kangqiang; Jiang, Xiue; Li, Shang

doi:10.1021/acsami.2c11874

Cited by 10 publications

(7 citation statements)

References 59 publications

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“…This distinct behavior was attributed to differences in the binding mode between AuECYN and AuMBA toward thrombin. However, future investigations will need to evaluate more systematically the influence of exposure time, usGNP surface chemistry (including ligand type, charge, density, and chirality), ,, and protein structural and thermodynamic properties on the conformation and function of interacting proteins. A combination of experimental and computational approaches will also be paramount to allow further progress in this area. − …”

Section: Resultsmentioning

confidence: 99%

Time Evolution of Ultrasmall Gold Nanoparticle–Protein Interactions

et al. 2023

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To date, much effort has been devoted toward the study of protein corona formation onto large gold nanoparticles (GNPs). However, the protein corona concept breaks down for GNPs in the ultrasmall size regime (<3 nm), and, as a result, our understanding of ultrasmall GNP (usGNP)–protein interactions remains incomplete. Herein, we used anionic usGNPs and six different proteins as model systems to systematically investigate usGNP–protein interactions, with particular focus on the time evolution and long-term behavior of complex formation. The different proteins comprised chymotrypsin (Cht), trypsin (Try), thrombin (Thr), serum albumin (HSA), cytochrome c (Cyt c), and factor XII (FXII). We used a range of biochemical and biophysical methods to estimate binding affinities, determine the effects of usGNPs on protein structure and function, assess the reversibility of any protein structural and functional changes, and evaluate usGNP–protein complex stability. Among the main findings, we observed that prolonged (24 h)but not short-term (10 min)interactions between proteins and usGNPs permanently altered protein function, including enzyme activities (Try, Thr, and FXIIa), peroxidase-like activity (Cyt c), and ligand-binding properties (HSA). Remarkably, this occurred without any large-scale loss of the native global conformation, implying time-dependent effects of usGNPs on local protein conformation or dynamics. We also found that both short-(10 min) and long-term (24 h) interactions between proteins and usGNPs yielded short-lived complexes, i.e., there was no time-dependent “hardening” of the interactions at the binding interface as usually seen with large GNPs. The present study increases our fundamental understanding of nano-bio interactions in the ultrasmall size regime, which may assist the safe and effective translation of usGNPs into the clinic.

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Section: Resultsmentioning

confidence: 99%

Time Evolution of Ultrasmall Gold Nanoparticle–Protein Interactions

et al. 2023

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“…Khang et al showed that the highly unfolded proteins in the protein corona activated a much more severe immune response, but serum proteins with negligible structural changes did not. In addition, the evolution of the in vivo protein corona is also worth identifying since it may also affect the immune response during the in vivo journey of nanoparticles. , The metabolism of nanoparticles is the final stage regarding the fate of nanoparticles influenced by the protein corona. Although it did not attract significant attention, one consensus is its high relevance to the protein corona composition and biodistribution sites .…”

Section: Features Of the In Vivo Protein Corona Formation Of Nanopart...mentioning

confidence: 99%

Perspectives on Protein–Nanoparticle Interactions at the In Vivo Level

He,

Qu,

Shang

2024

Langmuir

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The distinct features of nanoparticles have provided a vast opportunity of developing new diagnosis and therapy strategies for miscellaneous diseases. Although a few nanomedicines are available in the market or in the translation stage, many important issues are still unsolved. When entering the body, nanomaterials will be quickly coated by proteins from their surroundings, forming a corona on their surface, the so-called protein corona. Studies have shown that the protein corona has many important biological implications, particularly at the in vivo level. For example, they can promote the immune system to rapidly clear these outer materials and prevent nanoparticles from playing their designed role in therapy. In this Perspective, the available techniques for characterizing protein−nanoparticle interactions are critically summarized. Effects of nanoparticle properties and environmental factors on protein corona formation, which can further regulate the in vivo fate of nanoparticles, are highlighted and discussed. Moreover, recent progress on the biomedical application of protein corona-engineered nanoparticles is introduced, and future directions for this important yet challenging research area are also briefly discussed.

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“…[162][163][164] To visualize the exchange with NP sizing experiments, the two proteins must have markedly different sizes; alternatively, fluorescence labeling can be used. [156,165] Notably, as the Vroman effect can accelerate the desorption of a protein that binds persistently on its own (see Subsubsection 2.2.3, Figure 4), [88] a competition experiment bears the risk of inducing rather than proving reversible binding of the protein under study.…”

Section: Soft Coronamentioning

confidence: 99%

“…For example, 19 F diffusion-ordered nuclear magnetic resonance (NMR) spectroscopy is a diffusion-based technique applicable to turbid media. [154] Two other recently proposed, spectroscopy-based in-situ methods are Förster resonance energy transfer (FRET) [155,156] and synchrotron-radiation far-UV circular dichroism (CD) spectroscopy. [157] Fluorescence imaging within microfluidic devices is an elegant technique that allows in-situ tracking of protein adsorption in space/time along a flow channel after mixing NPs and fluorescently labeled proteins.…”

Section: Soft Coronamentioning

confidence: 99%

Mechanistic Understanding of Protein Corona Formation around Nanoparticles: Old Puzzles and New Insights

Nienhaus

2023

Small

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Although a wide variety of nanoparticles (NPs) have been engineered for use as disease markers or drug delivery agents, the number of nanomedicines in clinical use has hitherto remained small. A key obstacle in nanomedicine development is the lack of a deep mechanistic understanding of NP interactions in the bio‐environment. Here, the focus is on the biomolecular adsorption layer (protein corona), which quickly enshrouds a pristine NP exposed to a biofluid and modifies the way the NP interacts with the bio‐environment. After a brief introduction of NPs for nanomedicine, proteins, and their mutual interactions, research aimed at addressing fundamental properties of the protein corona, specifically its mono‐/multilayer structure, reversibility and irreversibility, time dependence, as well as its role in NP agglomeration, is critically reviewed. It becomes quite evident that the knowledge of the protein corona is still fragmented, and conflicting results on fundamental issues call for further mechanistic studies. The article concludes with a discussion of future research directions that should be taken to advance the understanding of the protein corona around NPs. This knowledge will provide NP developers with the predictive power to account for these interactions in the design of efficacious nanomedicines.

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Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Cited by 10 publications

References 59 publications

Time Evolution of Ultrasmall Gold Nanoparticle–Protein Interactions

Time Evolution of Ultrasmall Gold Nanoparticle–Protein Interactions

Perspectives on Protein–Nanoparticle Interactions at the In Vivo Level

Mechanistic Understanding of Protein Corona Formation around Nanoparticles: Old Puzzles and New Insights

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