DNA–melamine hybrid molecules: from self-assembly to nanostructures

• Rina Kumari,
• Shib Shankar Banerjee,
• Anil K. Bhowmick and
• Prolay Das

Beilstein J. Nanotechnol. 2015, 6, 1432–1438, doi:10.3762/bjnano.6.148

• phosphoramidation cross coupling was confirmed by polyacrylamide gel electrophoresis (PAGE), reversed phase high performance liquid chromatography (RP-HPLC), matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) mass spectrometry (MS). The reaction products were purified by dialysis

Peptide-equipped tobacco mosaic virus templates for selective and controllable biomineral deposition

• Klara Altintoprak,
• Axel Seidenstücker,
• Alexander Welle,
• Sabine Eiben,
• Petia Atanasova,
• Nina Stitz,
• Alfred Plettl,
• Joachim Bill,
• Hartmut Gliemann,
• Holger Jeske,
• Dirk Rothenstein,
• Fania Geiger and
• Christina Wege

Beilstein J. Nanotechnol. 2015, 6, 1399–1412, doi:10.3762/bjnano.6.145

• . Covalent conjugation of peptides was confirmed for both single CPs and intact TMV particles by denaturing and native gel electrophoresis, respectively. Peptide modification of CPs resulted in a band shift with respect to increasing molecular weight, as compared to nonmodified CP in denaturing sodium

• dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) (Figure 2a). The efficiency of peptide conjugation was determined by the ratio of the band intensities of modified and nonmodified CPs after Coomassie Blue staining. The binding efficiencies to individual CP subunits were ≈60% for all

• investigated peptides, corresponding to about 1250 peptides exposed on every 300 nm rod. The molecular weights of the differently modified CPs were in good agreement with the values calculated for the distinct conjugates (Table 2). The intact TMV particles were analyzed by native gel electrophoresis (0.9

Polymer blend lithography for metal films: large-area patterning with over 1 billion holes/inch²

• Cheng Huang,
• Alexander Förste,
• Stefan Walheim and
• Thomas Schimmel

Beilstein J. Nanotechnol. 2015, 6, 1205–1211, doi:10.3762/bjnano.6.123

• plasmons; Introduction Research on micro-/nano-sized island arrays and perforated films has drawn wide interest due to their applications in various fields, such as optical devices [1][2], DNA or protein electrophoresis [3][4], and catalysis [5][6]. Varieties of techniques have been developed to achieve

Protein corona – from molecular adsorption to physiological complexity

• Lennart Treuel,
• Dominic Docter,
• Michael Maskos and
• Roland H. Stauber

Beilstein J. Nanotechnol. 2015, 6, 857–873, doi:10.3762/bjnano.6.88

• polyacrylamide gel electrophoresis (1D-/2D-PAGE) [28][91][92][93][94][95][96][97][98]. Recently, Tenzer et al. [8][99] introduced an intriguing combination of 1D-/2D-PAGE and immune-blotting with sophisticated label-free liquid chromatography mass spectrometry (LC-MS) and demonstrated the unique abilities of

Mechanical properties of MDCK II cells exposed to gold nanorods

• Anna Pietuch,
• Bastian Rouven Brückner,
• David Schneider,
• Marco Tarantola,
• Christina Rosman,
• Carsten Sönnichsen and
• Andreas Janshoff

Beilstein J. Nanotechnol. 2015, 6, 223–231, doi:10.3762/bjnano.6.21

• ), respectively. The following day, excess PEG in solution was removed by centrifugation of the suspension and PEGylation was confirmed by gel electrophoresis [10][13][25]. Concentration of particles is given as concentration of gold in μg/mL or particle number per mL. Fluorescence and dark field imaging

Caveolin-1 and CDC42 mediated endocytosis of silica-coated iron oxide nanoparticles in HeLa cells

• Nils Bohmer and
• Andreas Jordan

Beilstein J. Nanotechnol. 2015, 6, 167–176, doi:10.3762/bjnano.6.16

• . Knockdown efficiency To demonstrate effective knockdown of target proteins, transfected cells were collected in every single experiment. The expression level of target proteins was determined in comparison to non-transfected control cells by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS

Functionalization of α-synuclein fibrils

• Simona Povilonienė,
• Vida Časaitė,
• Virginijus Bukauskas,
• Arūnas Šetkus,
• Juozas Staniulis and
• Rolandas Meškys

Beilstein J. Nanotechnol. 2015, 6, 124–133, doi:10.3762/bjnano.6.12

• ANX column and reloaded into a Q XL column. A typical yield from 1 L of culture was 30 mg of the homogenous protein. A band corresponding to an 18 kDa protein was observed in 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) (Figure 1). The theoretical molecular mass of α

• , was used for control assays. Protein purity was evaluated by gel electrophoresis. Mass spectrometry verified the presence of the cysteine residue in the C terminal. α-SynC141 and α-Syn fibril formation Lyophilized proteins were dissolved in the buffer: 50 mM Tris-HCl, 100 mM NaCl, pH 7.5 to a final

The fate of a designed protein corona on nanoparticles in vitro and in vivo

• Denise Bargheer,
• Julius Nielsen,
• Gabriella Gébel,
• Markus Heine,
• Sunhild C. Salmen,
• Roland Stauber,
• Horst Weller,
• Joerg Heeren and
• Peter Nielsen

Beilstein J. Nanotechnol. 2015, 6, 36–46, doi:10.3762/bjnano.6.5

• (EDC) to covalently bind PEG to the particles which diminished or even reversed the charge as seen in electrophoresis (Figure 1) [26]. By modifying the EDC concentration, partly or completely PEGylated species could be obtained. Size exclusion chromatography and DLS showed the increase of the size

• , electrophoresis the change in charge of the particles (Figure 1). In vitro experiments For in vitro experiments, a selection of these nanoparticles was incubated first with the test protein transferrin to perform a corona which was then replaced by albumin or plasma proteins. The adsorbed corona was compared in

• resulted in a more neutral particle (B), reaction with PEG-bisamine in an even cationic particle (C) as seen in electrophoresis (left Quantum dots, right SPIOs with the same polymer-coating and the same pegylation). Modification of the EDC concentration resulted in gradually PEGylated products, which can

Mammalian cell growth on gold nanoparticle-decorated substrates is influenced by the nanoparticle coating

• Christina Rosman,
• Sebastien Pierrat,
• Marco Tarantola,
• David Schneider,
• Eva Sunnick,
• Andreas Janshoff and
• Carsten Sönnichsen

Beilstein J. Nanotechnol. 2014, 5, 2479–2488, doi:10.3762/bjnano.5.257

• obtained from gel electrophoresis for PEG particles can be found in the Supporting Information of [20]. Live cell imaging In order to investigate how single MDCK II cells adhere and grow on nanoparticle-decorated substrates, live cell imaging using optical dark field microscopy was performed. For

• –PEG particles) or 75% COOH–PEG–SH and 25% CH3O–PEG–SH (COOH–PEG particles), respectively. The next day, excess PEG was removed by centrifugation. The success of the PEGylation was tested by gel electrophoresis, which also reveals the surface charge of the particles (Supporting Information of [20

In vitro and in vivo interactions of selected nanoparticles with rodent serum proteins and their consequences in biokinetics

• Wolfgang G. Kreyling,
• Stefanie Fertsch-Gapp,
• Martin Schäffler,
• Blair D. Johnston,
• Nadine Haberl,
• Christian Pfeiffer,
• Jörg Diendorf,
• Carsten Schleh,
• Stephanie Hirn,
• Manuela Semmler-Behnke,
• Matthias Epple and
• Wolfgang J. Parak

Beilstein J. Nanotechnol. 2014, 5, 1699–1711, doi:10.3762/bjnano.5.180

• -separation by gel electrophoresis. Negative controls were performed on the test tube used for the last washing step as well as on control incubations without any AuNP. For protein identification a MALDI-TOF MS proteomics analyzer was used. Furthermore, proteins in gel bands were analyzed quantitatively by

• protein densitometry. Only predominantly binding serum proteins could be analyzed by this quantitative approach. A typical electrophoresis gel visualized by Coomassie staining is given in Figure 2, which shows a variety of proteins present in the corona of the three differently sized AuNP. Proteins cover

• buffer and SDS-polyacrylyamide gel electrophoresis (PAGE) was carried out. Thereafter, gel lanes were dissected in smaller units and prepared for liquid chromatography mass spectroscopy/mass spectroscopy (LC–MS/MS analysis). Figure 5 shows the protein patterns of the most abundant proteins for all five

Different endocytotic uptake mechanisms for nanoparticles in epithelial cells and macrophages

• Dagmar A. Kuhn,
• Dimitri Vanhecke,
• Benjamin Michen,
• Fabian Blank,
• Peter Gehr,
• Alke Petri-Fink and
• Barbara Rothen-Rutishauser

Beilstein J. Nanotechnol. 2014, 5, 1625–1636, doi:10.3762/bjnano.5.174

• analyzed applying an ellipse fit. A total of 982 counts were performed for the NPs and 102 counts were collected for the micron-sized particles. The electrophoretic mobility of the particles was determined by electrophoresis (Brookhaven 90 Plus Instruments Corp., Holtsville, USA). The measured particle

Silica nanoparticles are less toxic to human lung cells when deposited at the air–liquid interface compared to conventional submerged exposure

• Alicja Panas,
• Andreas Comouth,
• Harald Saathoff,
• Thomas Leisner,
• Marco Al-Rawi,
• Michael Simon,
• Gunnar Seemann,
• Olaf Dössel,
• Sonja Mülhopt,
• Hanns-Rudolf Paur,
• Susanne Fritsch-Decker,
• Carsten Weiss and
• Silvia Diabaté

Beilstein J. Nanotechnol. 2014, 5, 1590–1602, doi:10.3762/bjnano.5.171

• (OptEIA kits, Heidelberg, Germany). 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid (HEPES) and the chemicals for sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) were from Carl Roth (Karlsruhe, Germany). For the Western blots Immobilon-P PVDF membranes (Millipore, Eschborn, Germany

• for 15 s and then stored at −20 °C. Equal amounts of the lysates were loaded onto 10% SDS-polyacrylamide gels and after electrophoresis, the proteins were transferred onto Immobilon-P PVDF membranes. The membranes were blocked with 5% (w/v) non-fat dry milk in 1% Tween20 in Tris-buffered saline (TBS

Protein-coated pH-responsive gold nanoparticles: Microwave-assisted synthesis and surface charge-dependent anticancer activity

• Dickson Joseph,
• Nisha Tyagi,
• Christian Geckeler and
• Kurt E.Geckeler

Beilstein J. Nanotechnol. 2014, 5, 1452–1462, doi:10.3762/bjnano.5.158

• using the ImageJ software. The hydrodynamic size and zeta potential were recorded by light scattering using ELS 8000 (Photal, Otsuka Electronics Co. Ltd, Japan). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed by using an electrophoretic apparatus (Amersham Biosciences

The cell-type specific uptake of polymer-coated or micelle-embedded QDs and SPIOs does not provoke an acute pro-inflammatory response in the liver

• Markus Heine,
• Alexander Bartelt,
• Oliver T. Bruns,
• Denise Bargheer,
• Artur Giemsa,
• Barbara Freund,
• Ludger Scheja,
• Christian Waurisch,
• Alexander Eychmüller,
• Rudolph Reimer,
• Horst Weller,
• Peter Nielsen and
• Joerg Heeren

Beilstein J. Nanotechnol. 2014, 5, 1432–1440, doi:10.3762/bjnano.5.155

• intravenous injection. As determined by DLS measurements, the sizes of QDs- or SPIOs-labelled lipid micelles are approximately 250 nm. After intravenous injection, lipid micelles are rapidly hydrolyzed to particles smaller than 100 nm in vivo [38]. Based on agarose gel electrophoresis, the surface charge of

The protein corona protects against size- and dose-dependent toxicity of amorphous silica nanoparticles

• Dominic Docter,
• Christoph Bantz,
• Dana Westmeier,
• Hajo J. Galla,
• Qiangbin Wang,
• James C. Kirkpatrick,
• Peter Nielsen,
• Michael Maskos and
• Roland H. Stauber

Beilstein J. Nanotechnol. 2014, 5, 1380–1392, doi:10.3762/bjnano.5.151

• bromophenol blue) to the pellet and incubation at 95 °C for 5 min. 1D SDS-PAGE Discontinuous SDS-polyacrylamide gel electrophoresis (PAGE) was carried out according to standard procedures [51]. Proteins were visualized by staining with Coomassie brilliant blue R-250 as described [52]. All experiments were

Surface processes during purification of InP quantum dots

• Natalia Mordvinova,
• Pavel Emelin,
• Alexander Vinokurov,
• Sergey Dorofeev,
• Artem Abakumov and
• Tatiana Kuznetsova

Beilstein J. Nanotechnol. 2014, 5, 1220–1225, doi:10.3762/bjnano.5.135

• method of purification, electrophoresis, is investigated and described in particular. Keywords: cadmium-free material; electrophoresis; luminescence; precipitation; purification; quantum dots; semiconductors; Introduction Colloidal semiconductor nanocrystals (NCs) have been studied extensively for the

• of a “bad” one [8]. Another simple and effective method widely used in biological and biochemical research, protein chemistry and pharmacology is electrophoresis [9]. Electrophoretic techniques can separate charged objects in a uniform electric field, but this technique is usually applied to aqueous

• acetone were separated by centrifugation and re-dissolved in toluene. Electrophoresis was carried out in acetone in an U-shaped quartz tube, the distance between two electrodes is 10 cm. The QDs were placed near the cathode and deposited on the anode made of stainless steel at the voltage of 1 kV and were

Nanostructure sensitization of transition metal oxides for visible-light photocatalysis

• Hongjun Chen and
• Lianzhou Wang

Beilstein J. Nanotechnol. 2014, 5, 696–710, doi:10.3762/bjnano.5.82

• are mainly two methods used to modify quantum dots on the surface of semiconductor. The first method is the in situ growth method. The second method is based on the ex situ assembly of pre-synthesized quantum dots by covalent bonding, electrostatic force or the external forces such as electrophoresis

The softening of human bladder cancer cells happens at an early stage of the malignancy process

• Jorge R. Ramos,
• Joanna Pabijan,
• Ricardo Garcia and
• Malgorzata Lekka

Beilstein J. Nanotechnol. 2014, 5, 447–457, doi:10.3762/bjnano.5.52

• analytical technique, which uses gel electrophoresis to separate native proteins, the same number of cells of about 2.56 × 106 cells per mL for each cell line was lysed and loaded on 12% gels for SDS-PAGE and afterwards transferred to a polyvinylidene difluoride membrane (Roche). After blocking with casein

• blot method: The Western blot technique is a standard technique used in cell biology to detect specific proteins in the sample. It follows through two steps. First, an electrophoresis is performed to separate proteins from a cell extract. Second, proteins are transferred to a membrane, on which they

Nanoscopic surfactant behavior of the porin MspA in aqueous media

• Ayomi S. Perera,
• Hongwang Wang,
• Tej B. Shrestha,
• Deryl L. Troyer and
• Stefan H. Bossmann

Beilstein J. Nanotechnol. 2013, 4, 278–284, doi:10.3762/bjnano.4.30

• procedure is described in detail in Supporting Information File 1. The hydrodynamic diameter and the zeta potential of the MspA aggregates were measured on a ZetaPALS Zeta Potential Analyzer (Brookhaven Instruments Corporation) by hydrodynamic light scattering and laser Doppler electrophoresis. One drop (50

Magnetic-Fe/Fe₃O₄-nanoparticle-bound SN38 as carboxylesterase-cleavable prodrug for the delivery to tumors within monocytes/macrophages

• Hongwang Wang,
• Tej B. Shrestha,
• Matthew T. Basel,
• Raj K. Dani,
• Gwi-Moon Seo,
• Sivasai Balivada,
• Marla M. Pyle,
• Heidy Prock,
• Olga B. Koper,
• Prem S. Thapa,
• David Moore,
• Ping Li,
• Viktor Chikan,
• Deryl L. Troyer and
• Stefan H. Bossmann

Beilstein J. Nanotechnol. 2012, 3, 444–455, doi:10.3762/bjnano.3.51

• hydrodynamic light scattering and laser Doppler electrophoresis. The 1H NMR and 13C NMR were obtained on a Varian Unity Plus (400 MHz) NMR spectrometer with deuterated chloroform or DMSO as solvents and TMS as the internal standard. ESI–MS spectra were acquired on an API4000 (Applied Biosystems, Foster City

Detection of interaction between biomineralising proteins and calcium carbonate microcrystals

• Hanna Rademaker and
• Malte Launspach

Beilstein J. Nanotechnol. 2011, 2, 222–227, doi:10.3762/bjnano.2.26

• proteins or protein fragments visible in lane P on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in Figure 3. The protein solution was gel-filtered to remove the SDS and DTT. The obtained gel-filtered protein solution (lane gfP) shows the major bands on SDS-PAGE. The gel-filtered