Increasing throughput of AFM-based single cell adhesion measurements through multisubstrate surfaces

• Miao Yu,
• Nico Strohmeyer,
• Jinghe Wang,
• Daniel J. Müller and
• Jonne Helenius

Beilstein J. Nanotechnol. 2015, 6, 157–166, doi:10.3762/bjnano.6.15

• grown to ≈80% confluency were detached from culture flasks by trypsin/EDTA and washed off with measurement media (cell line-specific media supplemented with 20 mM HEPES) containing 10% FCS. Cells were pelleted (420 g for 90 s) and resuspended in measurement media. Petri dishes with PDMS masks were

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

• agent ethylenediaminetetraacetic acid (EDTA, 2 mL) for 10 min in the incubator. Then, EDTA was removed and cells were detached from the substrate by incubation with trypsin/EDTA (1 mL) for 10 min in the incubator. Trypsination was stopped by addition of medium (10 mL), which was removed afterward by

Coating with luminal gut-constituents alters adherence of nanoparticles to intestinal epithelial cells

• Heike Sinnecker,
• Katrin Ramaker and
• Andreas Frey

Beilstein J. Nanotechnol. 2014, 5, 2308–2315, doi:10.3762/bjnano.5.239

• mixture of a variety of substances, it contains, among others, digestive enzymes like trypsin or chymotrypsin and also considerable amounts of immunoglobulin A and mucin [30]. It is known that components of the intestinal fluid, e.g., digestive enzymes from the gut lumen, can be immobilized at the outer

Effect of silver nanoparticles on human mesenchymal stem cell differentiation

• Christina Sengstock,
• Jörg Diendorf,
• Matthias Epple,
• Thomas A. Schildhauer and
• Manfred Köller

Beilstein J. Nanotechnol. 2014, 5, 2058–2069, doi:10.3762/bjnano.5.214

• Technologies) and detached from the culture flasks by the addition of 0.2 mL·cm−2 0.25% trypsin/0.05% ethylenediaminetetraacetic acid (EDTA, Sigma-Aldrich, Taufkirchen, Germany) for 5 min at 37 °C. Subsequently, the hMSCs were collected and washed twice with RPMI1640/10% FCS. Determination of cellular Ag-NP

Imaging the intracellular degradation of biodegradable polymer nanoparticles

• Anne-Kathrin Barthel,
• Martin Dass,
• Melanie Dröge,
• Jens-Michael Cramer,
• Daniela Baumann,
• Markus Urban,
• Katharina Landfester,
• Volker Mailänder and
• Ingo Lieberwirth

Beilstein J. Nanotechnol. 2014, 5, 1905–1917, doi:10.3762/bjnano.5.201

• of ciprofloxacin (Fluka, Switzerland; 2 mg·mL−1, 0.6%). Cells were grown in 500 cm2 triple flasks (Nunc, Germany) in a humidified incubator at 37 °C and 5% CO2. The culture medium was changed twice a week. At confluence, cells were detached by 0.5% trypsin (Invitrogen, Germany) and seeded in the

• specified concentrations. Flow cytometry Flow cytometry was used for quantification of intracellular nanoparticles and for the analysis of cell viability. Similar to the procedures previously described [26], adherent cells were detached by trypsin (Gibco, Germany) and seeded in α-MEM at a density of 100 000

• , the cells were detached by trypsin and newly seeded out. At the specified residence times, the sapphire disks were removed from the wells and dipped into 1-hexadecane to remove the remaining medium. The disks were covered with aluminum disks to prevent squeezing of the cells and the sandwich was

Biocompatibility of cerium dioxide and silicon dioxide nanoparticles with endothelial cells

• Claudia Strobel,
• Martin Förster and
• Ingrid Hilger

Beilstein J. Nanotechnol. 2014, 5, 1795–1807, doi:10.3762/bjnano.5.190

• ) supplemented with SupplementMix (PromoCell GmbH, Germany). Both cell lines were cultured at 37 ºC in a 5% CO2 humidified environment and the growth medium was exchanged every 2–3 days. Once the cells reached 70–85% confluency they were subcultivated. To detach the cells, GIBCO® trypsin (Life Technologies GmbH

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

• ; Cfh: complement component factor h; Mug1: murinoglobulin 1; Pzp: pregnancy zone protein; Itih4: inter alpha-trypsin inhibitor, heavy chain 4; Gsn: gelsolin; Ahsg: alpha-2-HS-glycoprotein; Fn1: fibronectin 1; Alb: albumin; C3: complement component 3. Schematics of the analysis of quantitative NP

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

• , Switzerland) and 1% penicillin/streptomycin (Gibco, Luzern, Switzerland) and kept at 37 °C and 5% CO2. The A549 epithelial cells were split twice per week using trypsin (0.05% trypsin-EDTA, GIBCO, Switzerland). J774A.1 cells were sub-cultured using the scraping method, resuspended in the medium and finally

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

• Analytics (Z-PS-SIL-GFP-0.07, Landsberg am Lech, Germany). Dulbecco’s Modified Eagle Medium (DMEM), Roswell Park Memorial Institute medium (RPMI-1640), Hank’s Balanced Salt Solution (HBSS), Dulbecco’s Phosphate Buffered Saline without Ca2+ and Mg2+ (DPBS-/-), penicillin, streptomycin, and trypsin were from

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

• observed after the reaction for all of the proteins except trypsin (TRY) and glucose oxidase (GOX). The AuNPs formed in the presence of the different proteins were characterized by UV–vis spectroscopy (Figure 1). The addition of Ag ions played an important role in the formation of the AuNPs, which is

• histone (HIS), chicken egg white lysozyme (LYS), ovalbumin (OVA), bovine serum albumin (BSA), bovine hemoglobin (BHG), bovine gamma globulin (BGG), glucose oxidase (Aspergillus niger) (GOX), and trypsin (porcine pancreas, TRY), used for the experiments were obtained from Sigma (USA) as a lyophilized

Near-infrared dye loaded polymeric nanoparticles for cancer imaging and therapy and cellular response after laser-induced heating

• Tingjun Lei,
• Alicia Fernandez-Fernandez,
• Romila Manchanda,
• Yen-Chih Huang and
• Anthony J. McGoron

Beilstein J. Nanotechnol. 2014, 5, 313–322, doi:10.3762/bjnano.5.35

• -Aldrich (St. Louis, MI): Malic acid, 1,12-dodecanedioic acid (DDA), dimethylsulfoxide (DMSO > 99.9%, reagent grade), pluronic F-127, Dulbecco phosphate-buffered saline (DPBS), phosphate buffered saline (PBS), IR820, penicillin-streptomycin solution, tetrahydrofuran (THF) and trypsin-EDTA. Glycerol was

• with PBS and collected by incubating with trypsin for 5 min. The same number of cells were counted and incubated with CM-H2DCFDA in the dark. After 30 min, cells were briefly washed with PBS, and the intensity of DCF was measured by a flow cytometer (BD Accuri C6, NJ). Study of HIF-1 expression To

Magnetic nanoparticles for biomedical NMR-based diagnostics

• Huilin Shao,
• Tae-Jong Yoon,
• Monty Liong,
• Ralph Weissleder and
• Hakho Lee

Beilstein J. Nanotechnol. 2010, 1, 142–154, doi:10.3762/bjnano.1.17

• within the DEVD site, which led to a corresponding increase in T2 relaxation time (Figure 5c). This dissociation was not observed when a specific caspase-3 inhibitor was added. A similar reverse switching strategy has been used to detect trypsin, renin, and matrix metalloproteinase 2 activities [57