Nanoscope multimode 8

Manufactured by Bruker

Sourced in United States

The Nanoscope Multimode 8 is a versatile atomic force microscope (AFM) system designed for high-resolution imaging and nanoscale characterization of a wide range of samples. It provides precise control and measurement capabilities for researchers and scientists working in various fields, including materials science, biology, and nanotechnology.

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Lab products found in correlation

Scanasyst fluid, by Bruker (2 mentions) Peakforce hirs f a, by Bruker (2 mentions) Escalab 250xi, by Thermo Fisher Scientific (2 mentions) Nanoscope analysis software v1, by Bruker (1 mentions) Electrochemical workstation, by Zahner (1 mentions) Dm1750m, by Leica camera (1 mentions) Jem 2100f, by JEOL (1 mentions) Smartlab, by Rigaku (1 mentions) Jsm 6490, by JEOL (1 mentions) Hr800, by Horiba (1 mentions) Nanoscope 5 controller, by Bruker (1 mentions) Scanasyst air, by Bruker (1 mentions) Em uc7 ultramicrotome, by Leica camera (1 mentions) Mica disk, by Agar Scientific (1 mentions) Nanoscope analysis software, by Bruker (1 mentions) Snl 10 tips, by Bruker (1 mentions) Ptc 200 peltier thermal cycler, by Bio-Rad (1 mentions)

15 protocols using nanoscope multimode 8

Quantifying Adhesion Forces via Force-Distance AFM

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A NanoScope MultiMode 8 (Bruker) was operated (NanoScope software v9.1) to conduct FD-based AFM. MSCT-D probes [with calculated spring constants, using thermal tune (38 ), ranging from 0.024 to 0.043 N m⁻¹] were used to record 5 μm × 5 μm arrays of force curves in the force-volume (contact) mode with an approach velocity of 1 μm s⁻¹ and retraction velocities of 0.1, 0.2, 1, 10, and 20 μm s⁻¹, a ramp size of 500 nm, a maximum force of 500 pN, and no surface delay. The sample was scanned using a line frequency of 1 Hz, and 32 pixels were scanned per line (32 lines). All FD-based AFM measurements were conducted in PBS at ~25°C. Force curves were analyzed using the NanoScope analysis software v1.7 (Bruker). To ensure that the analyzed adhesive peaks correspond to adhesion events occurring between particles linked to the PEG spacer and the heparin surface, the retraction curves before bond rupture were fitted with the WLC model for polymer extension (39 (link)). The latter expressed the force-extension (F-x) relationship for semiflexible polymers and was described by the following equation, where l_P is the persistence length and L_c is the contour length

F = \frac{k_{b} T}{l_{P}} (\frac{1}{4 {(1 - \frac{x}{L_{c}})}^{2}} + \frac{x}{L_{c}} - 0.25)

Origin software (OriginLab) was used to fit histograms of rupture force distributions.

Delguste M., Zeippen C., Machiels B., Mast J., Gillet L, & Alsteens D. (2018). Multivalent binding of herpesvirus to living cells is tightly regulated during infection. Science Advances, 4(8), eaat1273.

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Comprehensive Characterization of WS2 Films

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Optical images were recorded by an optical microscope equipped with a CCD camera (Lecia, DM1750M). The morphology of the WS₂ film before and after laser treatment was characterized by scanning electron microscope (JEOL, JSM-6490). Field-emission transmission electron microscope (JEOL, JEM-2100F) were used to observe the nanoscale morphology and crystal structure of thin solid film samples before and after laser treatment. The surface topography and roughness of the thin films were examined under an atomic force microscope (Bruker, Nanoscope Multimode 8), and the crystalline compositions and heterojunction locations of the samples were evaluated via Raman spectroscopy (Horiba Jobin Yvon, HR800) with an excitation laser source of 488 nm. X-ray photoelectron spectroscopy (Thermo Scientific, ESCALAB 250Xi) was carried out with a monochromatic Al Kα source to investigate the chemical states of the thin film samples. Mott-Schottcky analysis was conducted using an electrochemical workstation (Zahner, Zennium) with a frequency of 1kHz in dark condition. The structural analysis and phase change of sample was examined by X-ray diffraction (XRD, Rigaku SmartLab) using Cu Kα radiation.

Ma S., Zeng L., Tao L., Tang C.Y., Yuan H., Long H., Cheng P.K., Chai Y., Chen C., Fung K.H., Zhang X., Lau S.P, & Tsang Y.H. (2017). Enhanced Photocatalytic Activity of WS2 Film by Laser Drilling to Produce Porous WS2/WO3 Heterostructure. Scientific Reports, 7, 3125.

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Nanoscale Morphology Characterization of Organic Blends

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Atomic force microscopy images of TQ1, N2200, and the blend thin films were obtained with Nanoscope Multimode 8 (Bruker, USA) in PeakForce Tapping mode (ScanAsyst), controlled by Nanoscope 9.2 software, using a Si tip in air.
The blend films for AFM characterization were spin-coated on glass substrates at 1000 rpm from solutions with at total solute concentration of 10 mg/ml. After coating, the films were heated to 250 °C for 1 minute to ensure complete solvent evaporation, followed by thermal annealing at 120 °C for 10 minutes. When reference blend films were spun from chloroform, no pre-annealing was necessary, due to the high vapor pressure of chloroform. The weight ratio of TQ1:N2200 was 1:1 and 2:1.

Jalan I., Lundin L, & van Stam J. (2019). Using Solubility Parameters to Model More Environmentally Friendly Solvent Blends for Organic Solar Cell Active Layers. Materials, 12(23), 3889.

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Glycocluster Inhibition of SARS-CoV-2 Binding

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A Nanoscope Multimode 8 (Bruker) was operated in force-volume (contact) mode to conduct the force spectroscopy experiments on model surfaces (Nanoscope software v9.1). MSCT-D probes (nominal spring constant of 0.03 N m⁻¹) were used to record 5 μm × 5 μm maps, with a ramp size of 200 nm, a maximum force of 500 pN, and no surface delay. The sample was scanned using a line frequency of 1 Hz, and 32 pixels per line (32 lines). Both approach and retraction speed were kept constant at 1 µm s⁻¹.
To study the inhibitory potential of the synthesized 9-AcSA-derived glycoclusters on the binding affinity between SARS-CoV-2 and 9-Ac-SA, binding probabilities (fraction of curves showing binding events) were measured before and after incubation with different concentrations (0, 1, 10, and 100 µM respectively; additionally, at 1, 10, and 100 nM for porphyrin 11) of the four SA-/ and 9-AcSA-oligomers. Briefly, three force-volume maps were recorded on three different areas as described previously in the absence of any oligomer. Thereafter, the oligomer was added to the fluid cell and three maps were recorded for each concentration.

Petitjean S.J., Chen W., Koehler M., Jimmidi R., Yang J., Mohammed D., Juniku B., Stanifer M.L., Boulant S., Vincent S.P, & Alsteens D. (2022). Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection. Nature Communications, 13, 2564.

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Surface Roughness Analysis of CoCr Alloys

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AFM was used to examine the changes in surface roughness induced by different treatments of the CoCr surfaces. The AFM experiments were performed at ambient conditions on AFM instrument: a Nanoscope Multimode 8 equipped with a Nanoscope V controller (Bruker, Santa Barbara, CA). The topographies were acquired in ScanAsyst mode and Nanoscope 8.15r3 software. In ScanAsyst mode, silicon nitride cantilevers (ScanAsyst-Air Bruker) with a nominal spring constant of 0.4 N m⁻¹, a nominal resonance frequency of 50–90 kHz, and a nominal tip radius of 2 nm were used for imaging in air. AFM image analysis was performed using WSxM, 69 Nanoscope Analysis 1.4 software.

Mezour M.A., Oweis Y., El-Hadad A.A., Algizani S., Tamimi F, & Cerruti M. (2018). Surface modification of CoCr alloys by electrochemical reduction of diazonium salts. RSC Advances, 8(41), 23191-23198.

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Nanoscale Surface Characterization by FD-based AFM

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A Nanoscope Multimode 8 (Bruker) was operated (Nanoscope software v9.1) in the PeakForce QNM mode to conduct FD-based AFM. The AFM was equipped with a 120-μm piezoelectric scanner. Overview images (10 × 10 μm²) were recorded at imaging forces of ~150 pN, the AFM tip was oscillated vertically at 2 kHz, applying a 30- to 50-nm amplitude, the sample was scanned using a line frequency of 1 Hz, and 512 pixels were scanned per line (512 lines). The best high-resolution AFM topographs and interaction maps showing a maximum signal-to-noise ratio and applied force errors <10 pN were obtained at imaging forces of ~150 pN, an oscillation frequency of 0.25 kHz, oscillation amplitudes from 30 to 50 nm and line-scanning frequencies ≤0.125 Hz. All FD-based AFM images were recorded in imaging buffer at ~27 °C. Images and force curves were analyzed using the Nanoscope analysis software v1.50 (Bruker).

Alsteens D., Pfreundschuh M., Zhang C., Spoerri P.M., Coughlin S.R., Kobilka B.K, & Müller D.J. (2015). Imaging G protein–coupled receptors while quantifying their ligand-binding free-energy landscape. Nature methods, 12(9), 845-851.

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Atomic Force Microscopy of E. coli OMVs

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OMVs produced from different E. coli MG1655 strains were adsorbed onto freshly cleaved mica for 15 min in DPBS buffer at room temperature. After adsorption, the sample was gently washed with fresh DPBS buffer for five times to remove non-adsorbed OMVs. Then OMVs were imaged using force-distance curve-based AFM (FD-based AFM) performed with an AFM (Nanoscope Multimode 8, Bruker) operated in PeakForce Tapping mode in buffer solution (DPBS) at room temperature^{59 (link)}. The AFM was equipped with a 120 μm piezoelectric J scanner and fluid cell. The images were recorded using two different AFM cantilevers: PEAKFORCE‐HiRs‐F‐A (Bruker) with a nominal spring constant of 0.4 N/m, a resonance frequency of ≈ 165 kHz in liquid, and a sharpened silicon tip with a nominal radius of ≈ 1 nm or SCANASYST-FLUID + (Bruker) with a nominal spring constant of 0.7 N/m, a resonance frequency of ≈ 150 kHz in liquid, and a sharpened silicon tip with a nominal radius of ≈ 2 nm. Before imaging, cantilevers were calibrated by ramping on the mica surface and the thermal tuning method. Images were recorded at 2 kHz oscillation frequency, by applying an imaging force of 100–120 pN with a vertical amplitude of 30 nm. The AFM was placed inside a home‐built acoustic isolated and temperature‐controlled box. Raw AFM images were processed using the AFM analysis software Nanoscope v.1.8 for levelling and flattening.

Manioglu S., Modaresi S.M., Ritzmann N., Thoma J., Overall S.A., Harms A., Upert G., Luther A., Barnes A.B., Obrecht D., Müller D.J, & Hiller S. (2022). Antibiotic polymyxin arranges lipopolysaccharide into crystalline structures to solidify the bacterial membrane. Nature Communications, 13, 6195.

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Atomic Force Microscopy of Reconstituted Liposomes

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MelB reconstituted liposomes were diluted (1:100) in 20 mM Tris-HCl, pH 7.5, 100 mM KCl imaging buffer and adsorbed onto freshly cleaved mica for 10 min. Subsequently, the sample was gently rinsed five times with imaging buffer to remove non-adherent proteoliposomes.^{56 (link)} The AFM (Nanoscope Multimode 8, Bruker) was placed in a temperature-controlled acoustic isolation box and equipped with a 120-μm piezoelectric J scanner. AFM topographs of the sample were recorded in an imaging buffer using force-distance curve-based AFM^{57 (link)} operated in peak-force tapping mode at ≈ 25 °C. AFM imaging was performed applying a 120 pN imaging force, an oscillation frequency of 2 kHz, and an oscillation amplitude of 30 nm. For imaging, we used AFM cantilevers (ScanAsyst Fluid+, Bruker Nano Inc.) having a nominal spring constant of 0.7 N m⁻¹, a resonance frequency of ≈ 150 kHz in liquid, and a sharpened silicon tip with a nominal radius of ≈ 2 nm. Images were flattened and leveled using the AFM analysis software (Nanoscope v.1.8, Bruker).

Blaimschein N., Hariharan P., Manioglu S., Guan L, & Müller D.J. (2022). Substrate-Binding Guides Individual Melibiose Permeases MelB to Structurally Soften and to Destabilize Cytoplasmic Middle-Loop C3. Structure (London, England : 1993).

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Nanoscale Visualization of GSDMD Oligomers

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Force–distance curve‐based AFM (FD‐based AFM) (Dufrene et al, 2013) was performed using a Nanoscope Multimode 8 (Bruker, Santa Barbara, USA) operated in the PeakForce Tapping mode. The AFM was equipped with a 120‐μm piezoelectric scanner and fluid cell. AFM cantilevers used (BioLever mini BL‐AC40, Olympus Corporation, Tokyo, Japan) had a nominal spring constant of 0.1 N m⁻¹, a resonance frequency of ≈110 kHz in liquid and sharpened silicon tip with a nominal radius of 8–10 nm. The FD‐based AFM topographs were recorded in AFM imaging buffer (150 mM NaCl, 20 mM Hepes, pH 7.8) and at room temperature as described (Pfreundschuh et al, 2014). The maximum force applied to image the samples was 70 pN, and the oscillation frequency and oscillation amplitude of the cantilever were set to 2 kHz and 40 nm, respectively. The AFM was placed inside a home‐built temperature controlled acoustic isolation box. For data analysis, we took unprocessed AFM topographs. Diameters of ring‐like GSDMD oligomers were measured from the highest protruding rim. Heights of GSDMD arcs, slits, and rings were measured from their highest protruding feature relative to the surface of the lipid membrane. GSDMD oligomers were classified to having formed transmembrane pores if the inside of the pore was at least 3.5 nm deeper compared to the surface of the surrounding lipid membrane.

Sborgi L., Rühl S., Mulvihill E., Pipercevic J., Heilig R., Stahlberg H., Farady C.J., Müller D.J., Broz P, & Hiller S. (2016). GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death. The EMBO Journal, 35(16), 1766-1778.

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Morphological Analysis of Polymer Blends

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The morphology of the blends was investigated using both scanning electron microscopy (SEM) and atomic force microscopy (AFM). The SEM used in the work was a Phenom ProX (Netherlands) set to an accelerating voltage of 10 kV. All specimens tested in the SEM were impact fracture surfaces from the Izod impact tests of the blends. Certain specimens were etched in chloroform for 24 hours to remove the PLA phase. Droplet analysis of SEM micrographs was performed using ImageJ software.
The AFM used in the study was a Bruker (USA) Nanoscope Multimode 8 in peak force quantitative nano-mechanical (PFQNM) mode. Samples were prepared for the AFM using a Leica (Germany) EM UC7 ultramicrotome with a diamond knife to produce smooth, flat regions for AFM scanning.

Codou A., Anstey A., Misra M, & Mohanty A.K. (2018). Novel compatibilized nylon-based ternary blends with polypropylene and poly(lactic acid): morphology evolution and rheological behaviour. RSC Advances, 8(28), 15709-15724.

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