Nanowizard 4 nanoscience afm

Manufactured by Bruker

Sourced in Germany

The NanoWizard 4 NanoScience AFM is an atomic force microscope designed for high-resolution imaging and analysis of surfaces at the nanoscale. It provides precise measurement capabilities for a wide range of applications.

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Gegqqhhlggakqagdv, by GenScript (1 mentions) Data processing software, by Bruker (1 mentions)

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NanoWizard 4 (46 citations) Nanowizard 4 AFM (19 citations) NanoWizard AFM (14 citations)

4 protocols using nanowizard 4 nanoscience afm

Single-Molecule Force Spectroscopy of Bacterial Cells

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Single-molecule force spectroscopy
(SMFS)^{32 (link)} was performed at room temperature
(20 °C), using a JPK NanoWizard 4 NanoScience AFM. CDSN cantilevers
were calibrated by the thermal noise method, yielding spring constants
ranging from 0.03 to 0.07 N.m^–1. Force–distance
curves were recorded on 500 nm × 500 nm areas on the top of single
bacterial cells, employing the force mapping mode with the following
parameters: 32 × 32 force curves, constant approach and retraction
speeds of 1 μm s^–1, ramp length of 1 μm,
applied force of 250 pN, and additional dwell time of 0 or 250 ms,
corresponding to an actual time of contact of ∼50 and 300 ms.
For dynamic force spectroscopy, the retraction speed was varied from
1 to 2.5, 5, and 10 μm s^–1. All force data
were analyzed with the JPK Data Processing software, and statistical
analysis was carried out using the Origin software (OriginPro 2021).

Paiva T.O., Viljoen A., da Costa T.M., Geoghegan J.A, & Dufrêne Y.F. (2022). Interaction of the Staphylococcus aureus Surface Protein FnBPB with Corneodesmosin Involves Two Distinct, Extremely Strong Bonds. ACS Nanoscience Au, 3(1), 58-66.

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Quantitative Bacterial Surface Imaging and Adhesion Probing

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AFM imaging was performed with bare MSCT-D cantilevers in PBS buffer using the Quantitative Imaging mode (approach and retract velocity of 40 μm s⁻¹, z length of 600 nm for whole bacteria, and 150 nm for high-resolution images). Average roughness values were obtained for second-order polynomial line-leveled, high-resolution images (256 pixels by 256 pixels, 300 nm by 300 nm) recorded on top of bacteria.
All SMFS experiments were carried out in PBS supplemented with 0.1% BSA, 1 mM CaCl₂, and 1 mM MgSO₄ using a JPK NanoWizard 4 NanoScience AFM. Force spectroscopy data were collected in force mapping (force-volume) mode using a constant approach and retraction velocity of 1 μm s⁻¹, a ramp length of 250 nm, a contact force set point and pause of 250 pN and 250 ms, respectively, a closed z-loop, and fast and slow scan axes of 250 nm (16 pixels) and 1 μm (64 pixels), respectively. For dynamic force spectroscopy (dfs) and contact-time versus binding frequency experiments, respectively, retraction velocity and contact pause were varied as indicated in the relevant figures.

Viljoen A., Vercellone A., Chimen M., Gaibelet G., Mazères S., Nigou J, & Dufrêne Y.F. (2023). Nanoscale clustering of mycobacterial ligands and DC-SIGN host receptors are key determinants for pathogen recognition. Science Advances, 9(20), eadf9498.

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Collagen Fibril Density Analysis

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CoCol gels were prepared as
indicated above but with a buffer of PBS to reduce building up of
salt during dehydration. Samples were deposited onto a pressure cleaned
silicon wafer using an adjustable micropipette, resulting in a thin
collagen layer on the solid substrate. The gel was dehydrated in an
incubator over 24 h and subsequently washed three times with distilled
water. A 10 × 10 μm² area of each sample was
imaged by a NanoWizard 4 NanoScience AFM (JPK Instruments, Germany),
using a cantilever with a frequency of 20 kHz and a spring constant
of 0.9 N m^–1 in the intermitted contact mode. Fibril
density was determined by counting the number of fibrils present in
a 5000 × 5000 pixel area. For each concentration, 108 areas were
allocated over three samples to determine overall fibril density.
Fibril density was classified as low (4–6 fibrils), medium
(7–10 fibrils), and high (11–13 fibrils) and determined
by separating the number of fibrils into three distinct groups. A
two-way ANOVA was used to obtain the statistics.

McCarthy E.M., Floyd H., Addison O., Zhang Z.J., Oppenheimer P.G, & Grover L.M. (2018). Influence of Cobalt Ions on Collagen Gel Formation and Their Interaction with Osteoblasts. ACS Omega, 3(8), 10129-10138.

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Bacterial Cell Surface Adhesion Mapping

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Single-molecule force spectroscopy (SMFS)²⁰ experiments were performed in PBS, at 20 °C, using a JPK NanoWizard®4 Nanoscience AFM. fH-functionalized cantilevers were calibrated by the thermal noise method, yielding spring constants in the 0.02–0.03 N m⁻¹ range. Force-distance curves were recorded on the top of single bacterial cells (500 × 500 nm areas), in force mapping mode (32 × 32 force curves) using constant approach and retraction speeds of 1 µm s⁻¹, 1.4 µm ramp length and applying a force of 250 pN. The contact time was 50 ms. Dynamic force spectroscopy experiments were performed by changing the retraction speed from 1 to 2.5, 5 and 10 µm s⁻¹. All force curves were analyzed using JPK Data Processing software (version 6.1.172), considering the last adhesion peak, which was fit using the worm-like chain model of polymer extension^{52 (link)}. For blocking assays, we used either α-chain fibrinogen peptide 561-575 (SKQFTSSTSYNRGDS, Genscript) or 17-mer ɣ-chain fibrinogen peptide (GEGQQHHLGGAKQAGDV, Genscript) at a final concentration of 0.5 mg mL⁻¹. Force maps were recorded on the top of the same cell before and after peptide injection.

Paiva T.O., Geoghegan J.A, & Dufrêne Y.F. (2023). High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion. Communications Biology, 6, 302.

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