Nanoscope 8 multimode afm

Manufactured by Bruker

Sourced in United States

The Nanoscope VIII Multimode AFM is an atomic force microscope designed for high-resolution imaging and analysis of surfaces at the nanoscale. It provides a versatile platform for a wide range of applications in materials science, biology, and nanotechnology. The instrument utilizes a cantilever-based probe to measure the topography and properties of a sample, enabling users to study surface features with sub-nanometer resolution.

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Lab products found in correlation

Nanoscope analysis software, by Bruker (1 mentions) Scanasyst air, by Bruker (1 mentions) Snl 10, by Bruker (1 mentions) Phi 5000 versaprobe, by Physical Electronics (1 mentions) Nanoscope software, by Bruker (1 mentions) Porous polycarbonate membrane, by Merck Group (1 mentions) Tap150a, by Bruker (1 mentions) Dimension icon, by Bruker (1 mentions) Nanoscope analysis software v1, by Bruker (1 mentions)

Close spelling variants of this product

Nanoscope V Multimode 8 AFM NanoScope MultiMode VIII AFM microscope Nanoscope Multimode 8 Multimode 8 AFM Multimode AFM Nanoscope 8 Multimode 8

11 protocols using nanoscope 8 multimode afm

AFM Characterization of Surface Morphology

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Five specimens prepared from either Ti or ceramic were randomly selected for surface morphology characterization using an AFM (NanoScope 8 MultiMode AFM, Bruker Nano Inc., Nano Surfaces Division, Santa Barbara, CA, USA). The measurements were performed in contact mode using silicon nitride levers (Bruker SCANASYST-AIR, USA) with a measurement area of 100 × 100 µm², and the scan format was set at 256 × 256 pixels. The central positioning area of each specimen was selected for analysis, and care was taken to relocate to the same area during measurements for both material groups. Digital images of the original measurements were used for morphological description with Bruker NanoScope Analysis software (Version 1.40). Two parameters, average roughness (R_ave) and root mean square roughness (R_rms) were adopted to characterize the surface topography.
The estimated surface free energy of the materials was analyzed with a Contact Angle Meter (DM-701, Kyowa Interface Science Co., Ltd., Tokyo, Japan) using three probe liquids (0.5–1 μL/drop)—de-ionized water, diiodomethane, and ethylene glycol at 21 °C, and relative humidity of 21%. The average contact angle values were then analyzed for surface free energy (mJ/m²), using vOGT [62 ].

Wei C.X., Burrow M.F., Botelho M.G., Lam H, & Leung W.K. (2020). In Vitro Salivary Protein Adsorption Profile on Titanium and Ceramic Surfaces and the Corresponding Putative Immunological Implications. International Journal of Molecular Sciences, 21(9), 3083.

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AFM Imaging of Fungal Conidia

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For AFM experiments, conidia were immobilized by mechanical trapping into isoporous polycarbonate membranes of 3 µm pore size (Millipore, Burlington, MA, USA), close to the dimension of the conidia. After filtering a spore suspension (20 mL; 10⁶ cells per mL), the filter was carefully rinsed three times in deionized water and cut (1 cm × 1 cm). The lower part was carefully dried on a sheet of tissue and the specimen was attached to a steel sample puck using a small piece of adhesive tape. A droplet of liquid was rapidly added on the filter to avoid cell desiccation and the mounted sample was then transferred into the AFM liquid cell. Experiments were performed in contact mode in liquid and at room temperature using a Nanoscope 8 Multimode AFM (Bruker, Santa Barbara, CA, USA). Oxide-sharpened microfabricated silicon nitride (Si₃N₄) AFM probes with triangular cantilevers of stiffness 0.01 N/m were selected (MSCT, Bruker, Santa Barbara, CA, USA).

Valsecchi I., Dupres V., Stephen-Victor E., Guijarro J.I., Gibbons J., Beau R., Bayry J., Coppee J.Y., Lafont F., Latgé J.P, & Beauvais A. (2017). Role of Hydrophobins in Aspergillus fumigatus. Journal of Fungi, 4(1), 2.

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Single-Molecule Force Probing of Protein Interactions

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For single-molecule experiments, force–distance curves were recorded at room temperature (20 °C) in PBS buffer (pH 7.4) with 1 mM CaCl₂ using a Nanoscope VIII Multimode AFM (Bruker Corporation, Santa Barbara, CA) with the above-mentioned functionalized tips and substrates. Protein-coated substrates (SAG, Fn, or Coll) were gently rinsed with five baths of PBS, and attached to a steel sample puck (Bruker Corporation) using a double-sided adhesive and mounted onto the AFM liquid cell. The spring constants of the cantilevers were typically in the range of 0.01–0.04 N/m, as determined by thermal noise method.⁸⁴ Force mapping was performed by collecting a 32 × 32 array of force–distance curves on a 1 × 1 μm² area of the protein surfaces. All force curves were recorded at ~100 ms contact time, with a maximum applied force of 250 pN and 1000 nm s⁻¹ approach and retraction speeds.

Sullan R.M., Li J.K., Crowley P.J., Brady L.J, & Dufrêne Y.F. (2015). Binding Forces of Streptococcus mutans P1 Adhesin. ACS nano, 9(2), 1448-1460.

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SMFS of FnBPA A Domain Interactions

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SMFS measurements using tips and substrates functionalized with FnBPA A domains were performed at room temperature (20°C) in TBS buffer plus 1 mM ZnCl₂ using a Nanoscope VIII Multimode AFM (Bruker Corporation, Santa Barbara, CA). Recombinant FnBPA A domain with a C-terminal His tag was immobilized onto cantilevers and substrates as follows. Silicon substrates were coated by thermal evaporation with a thin layer of Cr (5 nm) followed by a thin layer of gold (30 nm). Gold substrates and gold cantilevers (see above) were rinsed in ethanol, cleaned for 10 min by UV-ozone treatment, rinsed in ethanol, and dried with N₂. They were immersed overnight in a 0.1 mM solution of 99% HS-C₁₁-(EG)₃-OH thiols (ProChimia) and 1% HS-C₁₁-(EG)₃-NTA thiols (ProChimia), rinsed with ethanol, dried with N₂, and immersed in a 40 mM aqueous solution of NiSO₄ (pH 7.2) for 30 min. Cantilevers and substrates were then incubated in a 200-µl droplet of a 200-µg/ml solution of FnBPA A domains for 1 h and rinsed and stored in PBS. Unless stated otherwise, multiple force curves were recorded at 100-ms contact time, with a maximum applied force of 250 pN, and using a constant approach and retraction speed of 1,000 nm/s.

Herman-Bausier P., El-Kirat-Chatel S., Foster T.J., Geoghegan J.A, & Dufrêne Y.F. (2015). Staphylococcus aureus Fibronectin-Binding Protein A Mediates Cell-Cell Adhesion through Low-Affinity Homophilic Bonds. mBio, 6(3), e00413-15.

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AFM Imaging of Substrates in Liquid

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AFM images were recorded using
a commercial AFM (Nanoscope VIII MultiMode AFM, Bruker Nano Inc.,
Nano Surfaces Division, Santa Barbara, CA) equipped with a 150 μm
× 150 μm × 5 μm scanner (J-scanner). The glass
substrates were fixed on a steel sample puck using a small piece of
adhesive tape. Images were recorded in PBS buffer at room temperature
(∼22 °C) using the peak force tapping mode.^{57 (link)} For this purpose, a quartz fluid cell was used.
The mounted samples were immediately transferred into the AFM liquid
cell while avoiding dewetting. Oxide-sharpened microfabricated Si₃N₄ cantilevers were used (SNL-10, Bruker Nano Inc.,
Nano Surfaces Division, Santa Barbara, CA). The spring constants of
the cantilevers were measured using the thermal noise method, yielding
values around 0.2 N/m. The curvature radius of silicon nitride tips
was about 12 nm (manufacturer specifications). The deflection sensitivity
was calibrated by recording the response of the cantilever on a bare
glass substrate (cleaned as described above), considered as an infinitely
stiff surface. All topographic images shown in this article were flattened
using a third-order polynomial to correct surface tilt and eliminate
bow effects.

Quantin P., Colaço E., El Kirat K., Egles C., Ficheux H, & Landoulsi J. (2018). Layer-by-Layer Assembly of Nanosized Membrane Fractions for the Assessment of Cytochrome P450 Xenobiotic Metabolism. ACS Omega, 3(10), 12535-12544.

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Atomic Force Microscopy Imaging Protocol

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AFM images were recorded using a commercial AFM (NanoScope VIII MultiMode AFM, Bruker Nano Inc., Nano Surfaces Division, Santa Barbara, CA) equipped with a 150 × 150 × 5 μm scanner (J-scanner). The substrates were fixed on a stainless steel sample puck using a small piece of adhesive tape. Images were recorded in peak force tapping mode in air at room temperature (22-24 °C) using oxide-sharpened microfabricated Si3N4 cantilevers (Bruker Nano Inc., Nano Surfaces Division, Santa Barbara, CA). The spring constants of the cantilevers were measured using the thermal noise method, yielding values ranging from 0. 4 to 0.5 N/m. The curvature radius of silicon nitride tips was about 10 nm (manufacturer specifications). The raw data were processed using the imaging processing software NanoScope Analysis, mainly to correct the background slope between the tip and the surfaces.

Laurans M., Trinh K., Dalla Francesca K., Izzet G., Alves S., Derat E., Humblot V., Pluchery O., Vuillaume D., Lenfant S., Volatron F, & Proust A. (2020). Covalent Grafting of Polyoxometalate Hybrids onto Flat Silicon/Silicon Oxide: Insights from POMs Layers on Oxides. ACS applied materials & interfaces, 12(42).

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X-ray Photoelectron Spectroscopy of Peptide-Treated Titanium

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Ti substrate analyzed for XPS was carried out under high vacuum at room temperature. A Ti substrate was incubated in 1 mg/ml peptide solution (2 mL) for 2 h at room temperature. Peptide-treated samples were rinsed extensively with PBS and ultrapure water and dried under argon gas. XPS spectra were collected using a PHI 5000 VersaProbe (ULVAC-PHI, Chigasaki, Japan) system. All binding energies were calibrated using the C 1 s (285.0 eV). The morphology of PEP recruiting of the discs were scanned at 0.5 Hz rate in air using a NanoScope VIII Multimode AFM (Bruker Corporation, USA).

Li X., Liu Z., Xu S., Ma X., Zhao Z., Hu H., Deng J., Peng C., Wang Y, & Ma S. (2022). A drug delivery system constructed by a fusion peptide capturing exosomes targets to titanium implants accurately resulting the enhancement of osseointegration peri-implant. Biomaterials Research, 26, 89.

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Bacterial Surface Force Measurements

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Force measurements using hydrophobic tips were performed on a Nanoscope VIII Multimode AFM (Bruker Corporation, Santa Barbara, CA) at room temperature (20 °C) in M63 complete medium. Bacteria were immobilized by mechanical trapping (see above). A single cell was first localized using a silicon nitride tip, after which the tip was exchanged with a hydrophobic tip. Adhesion and rupture length histograms were obtained by recording 32 × 32 force–distance curves on areas of 500 × 500 nm on the bacterial pole surface. All force curves were recorded with a maximum applied force of 250 pN using a constant approach and retraction speed of 1.0 μm s^–1 and a contact time of 0.1 s.

Beaussart A., Baker A.E., Kuchma S.L., El-Kirat-Chatel S., O’Toole G.A, & Dufrêne Y.F. (2014). Nanoscale Adhesion Forces of Pseudomonas aeruginosa Type IV Pili. ACS Nano, 8(10), 10723-10733.

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Atomic Force Microscopy Imaging of Biofilms

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For imaging in air, AFM contact mode images were obtained at room temperature using a Nanoscope VIII Multimode AFM (Bruker Corporation, Santa Barbara, CA) with oxide-sharpened microfabricated Si₃N₄ cantilevers with a nominal spring constant of 0.01 N m^–1 (MSCT, Bruker Corporation). Force data were analyzed using the Nanoscope software (version 8.15, Bruker) and Matlab software (version R2013b). One hundred microliters of biofilm-induced cells was put in contact with freshly cleaved mica supports mounted on steel pucks. The samples were incubated for 2 h at 37 °C, gently rinsed in three successive baths of ultrapure water (Elga, purelab water), and allowed to dry at 30 °C overnight. For imaging in liquid, bacteria were immobilized by mechanical trapping into a polycarbonate porous membrane (Millipore) with a pore size similar to the cell size. After the cell suspension was filtered, the filter was gently rinsed in M63, carefully cut (1 cm × 1 cm), attached to a steel sample puck using a small piece of double-faced adhesive tape, the mounted sample transferred into the AFM liquid cell while avoiding dewetting, and imaged under minimum applied force using MSCT cantilevers.

Beaussart A., Baker A.E., Kuchma S.L., El-Kirat-Chatel S., O’Toole G.A, & Dufrêne Y.F. (2014). Nanoscale Adhesion Forces of Pseudomonas aeruginosa Type IV Pili. ACS Nano, 8(10), 10723-10733.

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Atomic Force Microscopy Characterization of Surfaces

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Atomic Force Microscopy (AFM) imaging was carried out using a commercial AFM (Dimension Icon, Bruker Co., Santa Barbara, CA, USA). The ScanAsyst mode was applied using a silicon tip (TAP150A, Bruker, nominal frequency of 150 kHz, nominal spring constant of 5 N/m) with a scan resolution of 512 samples per line at a scan rate of 1.0 Hz for an area 2.5 µm × 2.5 µm. Integral and proportional gains were optimized empirically during scanning. All post-image analysis was carried out using the built-in AFM software and Nanoscope Analysis (NanoScope VIII MultiMode AFM, Bruker Nano Inc., Nano Surfaces Division, Santa Barbara, CA, USA). Three randomly selected areas were scanned per sample and the results of roughness (root mean squared roughness, Rq) were presented as the mean ± standard deviation of three different samples for each group. The statistics used for contact angle analysis was a student t-test to distinguish statistical significance, p = 0.05.

Chen R., Curran J., Pu F., Zhuola Z., Bayon Y, & Hunt J.A. (2017). In Vitro Response of Human Peripheral Blood Mononuclear Cells (PBMC) to Collagen Films Treated with Cold Plasma. Polymers, 9(7), 254.

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