In Situ Characterization of the Protein Corona of Nanoparticles In Vitro and In Vivo

Latreille, Pierre‐Luc; Rabanel, Jean‐Michel; Goas, Marine Le; Salimi, Sina; Arlt, Jochen; Patten, Shunmoogum A.; Ramassamy, Charles; Hildgen, Patrice; Martinez, Vincent A.; Banquy, Xavier

doi:10.1002/adma.202203354

Cited by 19 publications

(10 citation statements)

References 84 publications

(116 reference statements)

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“…In addition to the centrifugation strategy, numerous technologies are developed recently and used to study the precise mechanism of corona formation, such as differential centrifugal sedimentation (DCS), FCS, DLS, differential dynamic microscopy (DDM), bio-layer interferometry (BLI), etc. [30][31][32][33][34][35][36][37][38] Nevertheless, it is still difficult for these technologies to resolve the detailed composition of the plasma protein corona. Notably, their pinpoint accuracy and sensitivity in detection will contribute to further enhancing the spatiotemporal resolution of nano-PPL to achieve the elaborate distinction between direct nanoparticleprotein interaction and indirect protein-protein interaction in the corona structure.…”

Section: Discussionmentioning

confidence: 99%

Fast and Dynamic Mapping of the Protein Corona on Nanoparticle Surfaces by Photocatalytic Proximity Labeling

et al. 2023

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Protein corona broadly affects the delivery of nanomedicines in vivo. Although it has been widely studied by multiple strategies like centrifugal sedimentation, the rapidly forming mechanism and the dynamic structure of the protein corona at the seconds level remains challenging. Here, a photocatalytic proximity labeling technology in nanoparticles (nano‐PPL) is developed. By fabricating a “core‐shell” nanoparticle co‐loaded with chlorin e6 catalyst and biotin‐phenol probe, nano‐PPL technology is validated for the rapid and precise labeling of corona proteins in situ. Nano‐PPL significantly improves the temporal resolution of nano‐protein interactions to 5 s duration compared with the classical centrifugation method (>30 s duration). Furthermore, nano‐PPL achieves the fast and dynamic mapping of the protein corona on anionic and cationic nanoparticles, respectively. Finally, nano‐PPL is deployed to verify the effect of the rapidly formed protein corona on the initial interaction of nanoparticles with cells. These findings highlight a significant methodological advance toward nano‐protein interactions in the delivery of nanomedicines in vivo.

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Section: Discussionmentioning

confidence: 99%

Fast and Dynamic Mapping of the Protein Corona on Nanoparticle Surfaces by Photocatalytic Proximity Labeling

et al. 2023

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“…[158] Recently, an interesting fluorescence image correlation-based approach dubbed differential dynamic microscopy (DDM) has proven to be effective for in situ protein corona studies. [124] Furthermore, small angle x-ray scattering (SAXS) [159,160] and neutron scattering (SANS) [161] enable NP sizing experiments via the structure factor.…”

Section: Soft Coronamentioning

confidence: 99%

“…[122] Similar layer thicknesses, in line with monolayer formation, were found for large (diameter 30-110 nm) PS NPs. [123,124] We have argued that dense grafting of blood proteins on NP surfaces should generate a hydrophilic, zwitterionic outer surface that minimizes further adsorption of proteins, as blood proteins are colloidally very stable. [107,125] On a critical note, the presence of a thin protein shell does not per se prove the presence of a monolayer.…”

Section: Monolayer or Multilayer?mentioning

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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“…This approach, named differential dynamic microscopy (DDM), relies on a fully automated and operator-independent procedure that calculates simultaneously for different wavevectors q the temporal correlations of the spatially Fourier-transformed sample images . DDM has been successfully demonstrated in a wide range of applications including the characterization of the Brownian dynamics of diluted , and concentrated , colloidal suspensions, the microrheology of complex fluids, – the active motion of swimming microorganisms ,, and crawling cells, the protein absorption on functionalized nanoparticles, and the diffusive behavior of large protein clusters …”

Section: Introductionmentioning

confidence: 99%

“…10 This approach, named differential dynamic microscopy (DDM), relies on a fully automated and operator-independent procedure that calculates simultaneously for different wavevectors q the temporal correlations of the spatially Fourier-transformed sample images. 11 DDM has been successfully demonstrated in a wide range of applications including the characterization of the Brownian dynamics of diluted 10,12 and concentrated 13,14 colloidal suspensions, the microrheology of complex fluids, 15−17 the active motion of swimming microorganisms 13,18,19 and crawling cells, 20 the protein absorption on functionalized nanoparticles, 21 and the diffusive behavior of large protein clusters. 22 The close formal correspondence with DLS enabled expanding the range of applicability of DDM by directly exploiting or adapting both well-established experimental geometries (like depolarized 23,24 or wide-angle scattering 25 to measure the rototranslational dynamics of anisotropic particles) and analytical tools (like cumulant expansions 22,24 to estimate polydispersity or even more refined inversion schemes, like CONTIN, 26 to access the particle size distribution).…”

Section: ■ Introductionmentioning

confidence: 99%

Protein Sizing with Differential Dynamic Microscopy

Guidolin,

Heim,

Adams

et al. 2023

Macromolecules

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Introduced more than 50 years ago, dynamic light scattering (DLS) is routinely used to determine the size distribution of colloidal suspensions as well as of macromolecules in solution, such as proteins, nucleic acids, and their complexes. More recently, differential dynamic microscopy (DDM) has been proposed as a way to perform DLS experiments with a microscope, with much less stringent constraints in terms of cleanliness of the optical surfaces but a potentially lower sensitivity due to the use of camera-based detectors. In this work, we push bright-field DDM beyond known limits and show it to be sufficiently sensitive to size small macromolecules in diluted solutions. By considering solutions of three different proteins (bovine serum albumin, lysozyme, and pepsin), we accurately determine the diffusion coefficient and hydrodynamic radius of both single proteins and small protein aggregates down to concentrations of a few milligrams per milliliter. In addition, we present preliminary results showing an unexplored potential for the determination of virial coefficients. Our results are in excellent agreement with those obtained in parallel with a state-of-the-art commercial DLS setup, showing that DDM represents a valuable alternative for rapid, label-free protein sizing with an optical microscope.

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In Situ Characterization of the Protein Corona of Nanoparticles In Vitro and In Vivo

Cited by 19 publications

References 84 publications

Fast and Dynamic Mapping of the Protein Corona on Nanoparticle Surfaces by Photocatalytic Proximity Labeling

Fast and Dynamic Mapping of the Protein Corona on Nanoparticle Surfaces by Photocatalytic Proximity Labeling

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

Protein Sizing with Differential Dynamic Microscopy

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