Anorganische Nanopartikel zum Transport von Nucleinsäuren in Zellen

Sokolova, Viktoriya; Epple, Matthias

doi:10.1002/ange.200703039

Cited by 40 publications

(9 citation statements)

References 214 publications

(226 reference statements)

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“…The desire to control and utilize the biological effects of NPs has sparked the development of a number of NP biomolecular conjugates including functionalisations with DNA, [22][23][24][25][26] peptides [22,27,28] and proteins. [29][30][31][32][33][34][35][36][37] Furthermore, NP-protein conjugates are used in many applications from sensing [38][39][40][41] and nanobiotechnology.…”

Section: Introductionmentioning

confidence: 99%

“…[29][30][31][32][33][34][35][36][37] Furthermore, NP-protein conjugates are used in many applications from sensing [38][39][40][41] and nanobiotechnology. [22,42] A number of experimental methods has been utilised in studying protein structures in solution [43] including circular dichroism, [44][45][46] Fourier transform infrared spectroscopy, [47][48][49] Raman spectroscopy/SERS [50,51] and fluorescence spectroscopy. [52,53] The structure of the BSA molecule is well characterised [54][55][56][57][58][59] making BSA a convenient model system for the study of NP/protein interactions.…”

Section: Introductionmentioning

confidence: 99%

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The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

et al. 2010

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Interactions between differently functionalised silver and gold nanoparticles (NPs) as well as polystyrene nanoparticles with bovine serum albumin (BSA) are studied using circular dichroism (CD) spectroscopy. It is found that the addition of NPs to the protein solution destroys part of the helical secondary structure of the protein as a result of surface adsorption. From the loss of free protein and hence the extent of their structural change adsorption equilibrium constants are derived. The results reveal that citrate‐coated gold and silver NPs exhibit much stronger interactions with BSA than polymeric or polymer‐coated metallic NPs. It is therefore concluded that for the particles considered, the influence of surface composition on the interaction behaviour dominates that of the core.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

et al. 2010

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“…[1] It has been reported that the nuclear import of proteins larger than 40 kD does not occur by passive diffusion. [2] Similarly, the nuclear import of macromolecules or particles is strictly regulated.…”

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confidence: 99%

Oligosaccharide‐Mediated Nuclear Transport of Nanoparticles

et al. 2008

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The transport of nanoparticles into the cellular nucleus is a potentially important technique because it can open the way to a wide range of applications, including the sequence-specific detection of genomic DNA, efficient DNA transfection, and the specific entry of drugs into the nucleus.[1] It has been reported that the nuclear import of proteins larger than 40 kD does not occur by passive diffusion.[2] Similarly, the nuclear import of macromolecules or particles is strictly regulated. Therefore, the nuclear import of nanoparticles that contain gold nanoparticles and quantum dots has been achieved by coating the surface with classical nuclear localization signals (NLS), that is, short, highly positively charged peptides.[3] However, the problem remains that positively charged particles can interact with serum protein, resulting in rapid clearance from the plasma compartment.[4] Because the cationic NLS interacts with negatively charged DNA, NLS peptides do not work as efficient signals for transport of DNA into the nucleus; [5] this implies that the use of peptide-based cationic NLS might be limited when using DNA-displaying nanoparticles.Monsigny et al. have shown that sugars can also work as nuclear localization signals. [6][7][8][9] The neoglycoproteins, BSA (bovine serum albumin)-glucose, BSA-mannose and BSA-fucose are rapidly transported into the nucleus of HeLa cells, whereas BSA without chemical modifications is not. Because carbohydrates normally show high biocompatibility and water solubility, they are suitable for use in the modification of synthetic carriers and nanoparticles. Previously, however, only the application of these carbohydrate signals to the nuclear import of proteins was examined, and there are no reports on the effectiveness of carbohydrate signals for the nuclear import of artificial materials, such as nanoparticles and polymers. Previous reports that used BSA have focused only on monosaccharides as a signal. In this paper, we expand the varieties of carbohydrates tested from monosaccharides to oligosaccharides in the search for an efficient signal that is applicable to the nuclear import of nanoparticles. Herein, we present our unique finding that nanoparticles (quantum dots) that display oligo a-glucopyranoside on their surface are readily transported into the nucleus of digitonin-permeabilized HeLa cells. Semiconductor QDs have a diameter of several nanometers and their specific transport inside the cell can be readily achieved through the display of multiple ligands on their surface. As far as we know, this is the first report to describe the import of nanoparticles into the nucleus without the use of cationic NLS.Because BSA that has been substituted with a-glucopyranoside has been reported to be efficiently transported into the cell nucleus, [6] we synthesized neoglycolipids that contain various carbohydrates comprised of different numbers of glucose units (Scheme 1). In addition to a-monoglucopyranoside-lipid 3, we synthesized maltose(Glca1-4Glc)-lipid 4, maltotriose(Glca1-4Glc...

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“…[2b,33] To examine the potential role of nanoparticle stabilisation of the functional protein in this work, we have generated and examined the impact of cellular exposure to particle formulations in which the protein was bound through a reductively [7b,27] or pH [4b,26] -cleavable linker, particle types (9) and (10). The pH or reductant-initiated cleavage of protein from these particles was initially confirmed (Figure S5 in the Supporting Information).…”

Section: Resultsmentioning

confidence: 99%

“…[6] In the vast majority of cases, particles taken up in this way are subsequently trapped within these compartments, unable to access the cytoplasm or nucleus or to directly influence cellular physiology. [7] From either gene transfection or protein delivery perspectives, payload access to the cytosol is a requirement; [7a,8] therefore, a number of approaches have been examined to facilitate the escape of nanoparticles or therapeutic agents from this default and highly acidic endo/lysosomal pathway. [2c,3a,9] In many cases this has been through engineering destructive or penetrating interactions with the endosome/lysosome membrane.…”

Section: Introductionmentioning

confidence: 99%

Engineering Cytochrome‐Modified Silica Nanoparticles To Induce Programmed Cell Death

Huang

Davies

Davis

2013

Chemistry A European J

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A low native membrane permeability and ineffective access to the cellular cytosol, together with aggressive proteolytic degradation, often severely hampers the practical application of any therapeutic protein or antibody. Through engineering the charging profile of mesoporous silica nanoparticles, cellular uptake and subsequent subcellular distribution can be controlled. We show herein that programmed cell death can subsequently be induced across a population of cancer cells with remarkable efficacy on conjugating a specific caspase-cascade-activating cytochrome to such cytosol-accessing particles.

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Anorganische Nanopartikel zum Transport von Nucleinsäuren in Zellen

Cited by 40 publications

References 214 publications

The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

Oligosaccharide‐Mediated Nuclear Transport of Nanoparticles

Engineering Cytochrome‐Modified Silica Nanoparticles To Induce Programmed Cell Death

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