Characterization of as-prepared graphitic sheets was performed by TEM, EDS, and AFM. Samples for TEM were prepared by first depositing a droplet of stock solution onto a carbon-free, 1000-mesh copper grid (Ted Pella Inc., CA USA) and allowing the sample to dry in air. TEM images were acquired using an EOL JEM-2100, operating at 200 kV. Chemical analysis of the graphitic sheets (using the TEM samples) was carried out by EDS using a JEOL JEM-3010 linked with an eXL-II energy dispersive X-ray analysis system at a resolution of 136 eV FWHM at 5.9 keV. AFM samples were prepared by depositing a droplet of stock solution onto a clean silicon surface at room temperature and allowing them to dry. Topographic AFM images were acquired using an MFP-3DTM AFM (Asylum Research, Santa Barbara, CA, USA) operated in AC “tapping” mode under ambient conditions. A silicon cantilever (Olympus, AC240TS) with a nominal spring constant of 2 Nm−1 was used for all images using a scan rate of 1.0 Hz and an image resolution of 512 × 512 pixels.
Ac240ts
Manufactured by Olympus
Sourced in Japan
The AC240TS is a high-performance analytical centrifuge designed for a variety of laboratory applications. It features a powerful motor that can achieve speeds up to 24,000 rpm, enabling efficient separation and isolation of samples. The centrifuge is equipped with a temperature control system that maintains the sample environment within a specified temperature range. The device is compatible with a wide range of rotor types and sample volumes, making it a versatile tool for research and diagnostic laboratories.
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Lab products found in correlation
Xe 100, by Park Systems (3 mentions)
Mfp 3d, by Oxford Instruments (3 mentions)
Jem 3010, by JEOL (1 mentions)
Mfp 3dtm afm, by Oxford Instruments (1 mentions)
Nanowizard 2 atomic force microscope, by Bruker (1 mentions)
Mfp 3d atomic force microscope, by Oxford Instruments (1 mentions)
Image j 5, by Media Cybernetics (1 mentions)
Thermal power sensor, by Thorlabs (1 mentions)
Imagej software version 5, by Media Cybernetics (1 mentions)
Cypher s, by Oxford Instruments (1 mentions)
Fv1000, by Olympus (1 mentions)
Mfp 3d biotm, by Oxford Instruments (1 mentions)
Live dead baclight bacterial viability kit, by Thermo Fisher Scientific (1 mentions)
Igor pro 6.22a, by Wavemetrics (1 mentions)
Aptes, by Merck Group (1 mentions)
Nanoscopemultimode 8 afm, by Bruker (1 mentions)
Ac160ts, by Olympus (1 mentions)
19 protocols using ac240ts
1
Characterization of Graphitic Sheets
2
Nanofiber Characterization by AFM
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Atomic force microscopy (AFM) was conducted to confirm nanofiber formation in peptide solutions [27 (link)]. 1K0 and 1K25 solutions at 0.01% (w/v) were prepared in 10 mM phosphate buffer, pH 7.4. Five microlitres of each solution was placed on a freshly cleaved muscovite mica substrate (V-1 quality; Emsdiasum, Hatfield, Pennsylvania, USA) and dried in a dessicator for 3 h minimum. A NanoWizard II atomic force microscope (JPK Instruments, Berlin, Germany) equipped with a cantilever was used in intermittent mode to probe samples. The 240 µm long silicon cantilever probe with aluminum reflex coating had a resonance frequency of 50–90 kHz, spring constant of 0.7–3.8 N/m, and tip radius of ≤7 nm (Olympus AC240TS, Tokyo, Japan). AFM images were collected from 5 different areas for each sample from 3 independent experiments and analyzed using the Gwyddion 2.2 software (Czech Metrology Institute, Brno, Czech Republic) to quantify nanofiber length and width.
3
Atomic Force Microscopy of Protein Complexes
4
Atomic Force Microscopy of Samples
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We used the MFP-3D-BIO Atomic Force Microscope system (Asylum Research) together with HQ-300-Au (Asylum Research) and AC240TS (Olympus) probes. In addition, we used the AC-mode in ambient conditions (partly in repulsive mode, ‘tapping mode’, and partly in attractive mode) and scanned an area of 1 μm2.
5
Investigating Surface Morphology of PEG-Au Composites
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The surface morphology of the pure PEG and PEG-Au composites was investigated by an MFP-3D atomic force microscope (Asylum Research, Santa Barbara, CA, USA). Firstly, 100 μL of each sample was cast in a silicon wafer and then allowed to air dry. Next, a silicon cantilever (Olympus AC240TS) with low-noise characteristics was applied to observe the topography maps, with the range of the spring constant approximately 2.0 N/m. Topography images were then captured in AC mode at 512 × 512 pixels, with the average roughness analyzed via Image J 5.0 software (Media Cybernetics Inc Rockville, MD, USA).
6
Atomic Force Microscopy of Mat Surfaces
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Atomic force microscopy (XE-100, Park Systems Corp, Mannheim, Germany) was used to study the surface structure of the mat samples by measuring the force between atoms, working under standard ambient environment. Surfaces of 5 μm × 5 μm of the mat samples were scanned, using a cantilever type Olympus AC240TS (f = 70 kHz; k = 2 N m−1) by non-contact measures surface topography, in the relatively larger distance between the tip and the sample surface. A charge coupled device (CCD) camera is aligned directly on the cantilever in order to provide high quality of the images. Differences in the surface morphology can be expressed in terms of various roughness parameters, such as: Arithmetic roughness (Ra) which represents the arithmetic mean of the height of peaks and depth of the valleys from a mean line, Rku (kurtosis)—characterizes the flatness of the surface distribution, Rsk (skewness)—characterizes the asymmetry of the surface distribution or root-mean-square roughness (Rq) [37 (link)]. These parameters were determined from five separate images of different locations of the surfaces of each mat samples.
7
Hierarchical Structures Morphology Analysis
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Micro- and nanoscale morphology measurements of the hierarchical structures were conducted on a commercial atomic force microscopy system (AFM, XE100—Park Systems, Suwon, Republic of Korea). The measurements were performed in non-contact mode, using standard cantilevers (AC240TS—Olympus Corporation, Tokyo, Japan; NCHR—Nanosensors, Neuchatel, Switzerland).
8
Tau and Heparin Aggregation Imaging
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Each sample was prepared by pipetting 30 μL (40 μM of tau plus 10 μM of heparin) in the presence or absence of 5 (10 μM and 1 μM respectively) onto highly orientated pyrolytic graphite (HOPG). The samples were incubated at room temperature for 30 min and then carefully washed. Atomic force microscopy imaging was performed in tapping mode using a Nanoscope III (Veeco, CA) and Olympus AC240TS cantilevers exhibiting spring constants of 2 N/m at resonance frequencies of 55 kHz. To achieve minimal imaging forces between AFM stylus and sample, the drive amplitude was set between 0.5 and 1.0 V, and the amplitude set point was adjusted manually to compensate for the thermal drift in order to maintain good tracking of the sample.
9
Lipid Monolayers for Protein Binding Studies
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Lipid monolayers were deposited using Langmuir-Blodgett transfer according to Baumann et al.38 (link). Briefly, freshly cleaved mica was immersed in the KSV Minitrough filled with 10 mM Na-Hepes, 150 mM NaCl, pH 7.0 at 37 °C before 20 μL of 1 mg/mL PBPS:PC (1:1) dissolved in chloroform was spread at the air-water interphase. The lipid monolayer was compressed at 5 mm/min to a surface pressure of 30 mN/m, which was recorded by a Wilhelmy plate. After 20 min stabilization, 3 nM hTH1 was injected under the compressed monolayer, allowed 30 min of equilibration, and then the mica was vertically pulled (5 mm/min) from the subphase buffer through the lipid film into air. Imaging was performed using a MFP-3D-BioTM atomic force microscope (Asylum research) in AC mode in air at room temperature using silicon cantilevers (AC240TS, Olympus) with a resonant frequency of ∼55 KHz and a ∼2 N/m spring constant. 256 × 256 pixels images were captured at a 0.5–1 Hz line scan rate.
10
Characterization of P1 Isomerization by AFM and UV/Vis
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AFM measurements were carried out with a NanoWizard III microscope (JPK Instruments AG, Germany). The AFM was operated in air at room temperature in tapping mode with silicon cantilevers (AC240TS, Olympus Corporation, Japan, spring constant 2 N/m). For UV/Vis spectroscopy, we used a setup consisting of a 75 W Xenon Lamp (LOT-QuantumDesign, GmbH, Germany), a fiber with a reflectance probe (LOT-QuantumDesign GmbH, Germany), and a spectrometer consisting of a spectrograph (Acton Series, Princeton Instruments) and a cooled CCD (Andor). All UV/Vis spectroscopy measurements presented in this paper have been performed under atmospheric pressure. E → Z isomerization of P1 was induced with a 365 nm high power UV LED (Thorlabs) with variable optical output and a FWHM of 12 nm. The light-intensity on the sample surface was measured with a thermal power sensor (Thorlabs).
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