Dnp s10

Manufactured by Bruker

Sourced in United States

The DNP-S10 is a Dynamic Nuclear Polarization (DNP) spectrometer designed and manufactured by Bruker. It is a specialized laboratory equipment used to enhance nuclear magnetic resonance (NMR) signals, enabling the study of materials and molecules at the atomic and molecular level.

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Lab products found in correlation

Nanowizard 3, by Bruker (1 mentions) Nanoscope iiia, by Veeco (1 mentions) Nanoscope iiia, by Digital Instruments (1 mentions) Nanowizard 2, by Bruker (1 mentions) Matlab, by MathWorks (1 mentions) Rtesp 300, by Bruker (1 mentions) Asylum mfp 3d, by Oxford Instruments (1 mentions) Plasma cleaner, by Diener Electronic (1 mentions) Nanoscope 5 controller, by Bruker (1 mentions) Jpk bioafm, by Bruker (1 mentions) Nanowizard 4, by Bruker (1 mentions) Lsr 2, by BD (1 mentions) Cell tak solution, by Corning (1 mentions)

9 protocols using dnp s10

Nanoscale Topography in Air and Water

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Atomic force microscopy
(AFM) measurements of the patterned structures in contact with air
were performed in tapping mode with the PicoPlus instrument (Molecular
Imaging, Agilent Technologies). The topography in contact with water
was observed in situ with the Nanowizard III (JPK Instruments, Germany)
using a temperature-controlled module consisting of a flow cell with
a Peltier element. Silicon nitride cantilevers DNP-S10 (Bruker) with
a nominal spring constant of 0.24 N m^–1 were utilized.
Height, diameter, and lateral spacing of the nanoscale features were
determined by employing Gwyddion free software.

Quilis N.G., Hageneder S., Fossati S., Auer S.K., Venugopalan P., Bozdogan A., Petri C., Moreno-Cencerrado A., Toca-Herrera J.L., Jonas U, & Dostalek J. (2020). UV-Laser Interference Lithography for Local Functionalization of Plasmonic Nanostructures with Responsive Hydrogel. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces, 124(5), 3297-3305.

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Quantitative Nanoscale Surface Characterization

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AFM experiments were carried out using a JPK NanoWizard IV microscope (Bruker, Billerica, MA, USA). Samples were analyzed in 1 mM or 1 M NaCl buffer depending on the solution used for the C₆-ssDNA self-assembly. Gold-coated Si cantilevers (DNP-S10, Bruker) with an elastic constant of 0.24 N/m and a tip radius of curvature of 10 nm were used for both shaving and imaging operation mode. Nanoshaving experiments were performed by scanning a selected area (typically a few µm wide) in hard tapping mode (setting a very small oscillating amplitude, typically 0.01 nm, with a free oscillation amplitude of 70–80 nm) to selectively displace molecules and obtain an exposed gold region. After the shaving, an image with larger scan size was acquired in both soft contact and Quantitative Imaging mode. QI mode is an imaging mode based on force spectroscopy: through the acquisition of a large set of force–distance curves, it allows reconstructing the sample topography from the z position of the tip at a specific force load. Since the tip is withdrawn from the surface between each pixel, there are almost no lateral forces, and dragging is avoided. The combination of imaging and force spectroscopy provides quantitative data on mechanical properties of the sample in addition to the height measurements.
Data have been analyzed with Gwyddion (v2.55) and JPKSPM Data Processing software.

Pinto G., Canepa P., Canale C., Canepa M, & Cavalleri O. (2020). Morphological and Mechanical Characterization of DNA SAMs Combining Nanolithography with AFM and Optical Methods. Materials, 13(13), 2888.

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Tapping Mode AFM Imaging of Muscovite Mica

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AFM imaging was done in tapping mode using a Nanoscope IIIa multimode AFM (Veeco, Santa Barabara, USA) employing a liquid cell with O-ring to prevent evaporation. Ten-millimetre muscovite discs (Agar Scientific) were glued with two-component epoxy glue onto metal pucks. Before sample loading, the mica was cleaved using sticky tape. Sharpened silicon nitride tips (DNP-S10, Bruker) with a force constant of 0.12 N m⁻¹ was used. Flattened images were constructed using WSxM 5.0 (Nanotec52 ) and Gwyddion53 . To minimize the force applied to the sample while scanning (and counter set point drifts in the system), the set point voltage was continuously adjusted to the lowest level for which tip-sample contact was maintained. Typical drive amplitudes were in the range 100–150 mV. It is important to stress that there is no correlation between the size of the cluster and our ability to resolve the individual molecules. The dominating parameter is the mobility of the molecules, be they isolated or clustered into islands, rather than the size of the cluster.

Sleutel M., Lutsko J., Van Driessche A.E., Durán-Olivencia M.A, & Maes D. (2014). Observing classical nucleation theory at work by monitoring phase transitions with molecular precision. Nature Communications, 5, 5598.

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Atomic Force Microscopy Force-Distance Measurements

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The force–distance
measurements were carried out by using a multimode atomic force microscope
with a maximum scan size of 130 × 130 μm². The
measurements were performed with a Nanoscope IIIa controller (Digital
Instruments, Santa Barbara, CA). A V-shaped cantilever made of silicon
nitride in the front and gold layer in the back for the reflection
of the laser beam (DNP-S10, Bruker) was utilized. The force–distance
data were acquired by conducting the tip extension and the tip retraction
in order. The rate of the tip movement was set up to be 0.5 mm/s for
both the approach and retraction periods. The number of replications
for each sample was 13. The rupture distance and adhesive force were
measured.

Yazdani-Ahmadabadi H., Felix D.F., Yu K., Yeh H.H., Luo H.D., Khoddami S., Takeuchi L.E., Alzahrani A., Abbina S., Mei Y., Fazli L., Grecov D., Lange D, & Kizhakkedathu J.N. (2022). Durable Surfaces from Film-Forming Silver Assemblies for Long-Term Zero Bacterial Adhesion without Toxicity. ACS Central Science, 8(5), 546-561.

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Atomic Force Microscopy of Amyloid and HDL

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Atomic force microscopy (AFM) imaging was performed using a Nanowizard II (JPK Instruments, Berlin) scanning probe microscope operating in tapping and contact mode in air. In tapping mode imaging of Aβ_1-42 fibrils, RTESP-300 (Bruker, United States) cantilevers were used with a nominal force constant of 40 N/m, a resonance frequency of 300 kHz, and a nominal tip radius 8 nm. For contact mode imaging of HDL subtypes, DNPS-10 (Bruker, United States) cantilevers were used with a nominal force constant of 0.06 N/m, and a nominal tip radius 10 nm. A detailed protocol used for the apoA-I-HDL characterization is supplied as Supplementary Information (see section “Characterization of HDL by AFM Imaging”). A wide range of areas of AFM images were analyzed using the commercial JPK image processing software and a customized image-analysis software (Matlab, MathWorks Inc, United States).

Dal Magro R., Simonelli S., Cox A., Formicola B., Corti R., Cassina V., Nardo L., Mantegazza F., Salerno D., Grasso G., Deriu M.A., Danani A., Calabresi L, & Re F. (2019). The Extent of Human Apolipoprotein A-I Lipidation Strongly Affects the β-Amyloid Efflux Across the Blood-Brain Barrier in vitro. Frontiers in Neuroscience, 13, 419.

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Stiffness Characterization of GelMA Hydrogels

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The stiffness of the GelMA hydrogels was measured using an atomic force microscope (AFM) (Asylum MFP-3D, Asylum Research, Santa Barbara, CA, USA) in contact force mode using silicon nitride cantilevers with a spring constant of 0.12 N/m (DNP-S10, Bruker, CA, USA). The tip geometry was triangular with a tip radius of 10 nm. Three samples were prepared for each sterilization method and three force maps of 10 μm × 10 μm were collected on each sample. Each force map was fitted to the linear region of the force curve to obtain the Young’s modulus using the Hertz Model and assuming the sample was isotropic and linearly elastic [16 (link)].

Lu T.T., Yan L.G, & Madri J.A. (1996). Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1.. Proceedings of the National Academy of Sciences of the United States of America, 93(21), 11808-11813.

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Supported Lipid Bilayer Formation and Protein Imaging

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The AFM cantilevers with a nominal spring constant of 0.24 N/m (DNP-S10, Bruker, Billerica, MA, USA) and the silica substrate were mounted inside a closed fluid cell with an O-ring. The 1 cm × 1 cm silica wafers (IMEC, Leuven, Belgium) were cleaned before using with the following procedure: sonication in 2% (w/w) SDS solution for 15 min, rinsing with ultrapure water, and drying under nitrogen stream. Finally, the substrates were treated by plasma cleaner (Diener electronic, Ebhausen, Germany). The lipid bilayers were formed by means of lipid vesicle fusion. 0.1 mg/mL of lipid vesicle solutions were incubated over the silica surface for at least 10 min and then the vesicle excess was rinsed from the chamber. Afterwards, the two Cyt2Aa2 proteins, wild type (WT) and the T144A mutant (25 µg/mL or 1.0 µM), were incubated with the lipid bilayers or with supported erythrocyte membrane for the desired experimental time. The surface topography was imaged in tapping mode with a JV-scanner controlled by a NanoScope V controller (Bruker, Billerica, MA, USA) at a scan rate of 1–2 Hz. The images were processed and analyzed with the Nanoscope program. The experiments were carried out at room temperature (298 K).

Tharad S., Promdonkoy B, & Toca-Herrera J.L. (2020). Protein-Lipid Interaction of Cytolytic Toxin Cyt2Aa2 on Model Lipid Bilayers of Erythrocyte Cell Membrane. Toxins, 12(4), 226.

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AFM Characterization of Macrophage Phagocytosis

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The atomic force microscopy (AFM) instrument used during all experiments is the Nanowizard 4™ with an automated stage (JPK BioAFM, Bruker). All force curves for Young's modulus measurements were acquired in contact mode using a colloidal probe, containing a spherical tip of 5 µm diameter (CP-qi-SCONT-BSG, force constant 0.1 N m -1 ) and using a setpoint of 2 nN at 2 µm s -1 . Viscoelastic properties were measured using the same AFM device equipped with a pyramidal tipped probe having a nominal radius of curvature of 10 nm (Force constant 0.3 N m -1 , DNP-S10; Bruker). During the viscoelasticity experiments, the cantilever oscillated with an amplitude of 50 nm at increasing frequencies (more specifically: 10,50,100,120,150 and 200 Hz). Processing of all AFM data was performed using JPK-Bruker software. finally, analysed by flow cytometry on the BD LSRII. Analysis was performed via FlowJo (v.10.8.1) software. The gating strategy was as follows: creating 'not debris' population from FSC x SSC, deriving F4/80+ population (representing BMDMs) from 'not debris' population, deriving CMFDA+ population from F4/80+ population (representing uptake of CMFDAstained MCA205 cells by BMDMs).

Van der Meeren L., Efimova I., Demuynck R., Parakhonskiy B., Krysko D.V, & Skirtach A.G. (2023). Mechanobiology of Ferroptotic Cancer Cells as a Novel "Eat-Me" Signal: Regulating Efferocytosis through Layer-by-Layer Coating. Advanced healthcare materials, 12(28).

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Atomic Force Microscopy of S. aureus

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S. aureus ATCC 29213 cells were investigated by AFM. Over-night culture growth, next-day dilutions and treatments were carried out as reported in Roncevic et al. [27] (link). Briefly, the bacteria were treated with 2 μM, 4 μM (corresponding to MIC and MBC) and 8 μM of the peptide-6 and incubated with shaking at 100 rpm at 37 °C for 1 h. The culture was then briefly centrifuged, and the pellet resuspended in one tenth of the supernatant. Melittin treated cells were prepared in the same way and treated with the peptide at 2 μM and 3.5 μM, corresponding to MIC and MBC respectively [28] (link). The control samples were prepared in the same fashion but without the peptide treatment. Bacterial adhesion to glass slides was enabled with Cell-Tak solution (Corning, NY, USA) coating [29] (link) as reported in [27] (link). AFM measurements were carried out in contact mode, under ambient conditions, using Bruker Multimode 3 (Digital Instruments, USA) instrument with a 0.12 N/m silicon-nitride probe (Bruker AFM probes USA, DNPS-10). Scan rates during imaging were kept between 2 and 3 Hz, and the image resolution was 512 pixels per line. Analysis of the obtained images was carried out with Gwyddion.

Rončević T., Krce L., Gerdol M., Pacor S., Benincasa M., Guida F., Aviani I., Čikeš-Čulić V., Pallavicini A., Maravić A, & Tossi A. (2019). Membrane-active antimicrobial peptide identified in Rana arvalis by targeted DNA sequencing. Biochimica et biophysica acta. Biomembranes, 1861(3).

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