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20 protocols using nsg01

1

Nanocellulose Morphology Characterization by AFM

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AFM was performed in tapping mode using NTEGRA Prima equipped with a NSG01 cantilever (NT-MDT, Russia) to examine the morphology of the nanocellulose samples. For sample preparation, the CNF/CCNF and the CNC suspensions were diluted to a concentration of 10 -2 and 10 -3 wt.%, respectively, and a droplet of each suspension was placed on a freshly cleaned silicon wafer substrate and dried. The AFM height images were then processed with the Gwyddion software. The nanoparticle diameter was determined from the height profiles of AFM height images as an average of 100 measurements.
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2

Atomic Force Microscopy of PLGA Nanoformulations

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The empty PLGA and nanoformulations were prepared for the Atomic Force Microscopy (AFM) experiments with a final concentration of 5 mg/mL. 20 μL drops of each suspension were deposited on 20 mm diameter mica discs sprayed with argon to avoid excess conglomeration of the NPs and the excess solvent was allowed to evaporate at room temperature. A NT-MDT Solver Pro microscope (Moscow, Russia), with single crystal silicon-antimony doped probe and a gold-coated tip (NSG-01 from NT-MDT) was used to collect images. The microscope was calibrated by a calibration grating (TGQ1 from NT-MDT) in order to reduce nonlinearity and hysteresis in the measurements. Scanning was performed in intermittent mode, with a frequency of 3 to 1 Hz. and the resolution of all the images acquired was 15 nm. The images were processed with the program Gwyddion and a statistical analysis over on the diameters of 30 different nanoparticles of each type was conducted to compare results to DLS data.
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3

Atomic Force Microscopy of Amyloid Fibrils

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Samples from the ThT aggregation assays at 90 h were diluted 10 times in MilliQ water and deposited onto freshly cleaved mica. After 15 min, the mica samples were rinsed 3–4 times with MilliQ water then dried completely under a gentle stream of nitrogen gas. The images were captured using an NTEGRA Prima setup (NT‐MDT, Moscow, Russia) at a resonance frequency around 180 kHz, using a gold‐coated single crystal silicon cantilever (NSG01, spring constant of ~5.1 N/m; NT‐MDT, Moscow, Russia). Images of 512 pixels were captured at a scan rate ranging from 0.3–0.5 Hz. Images were analyzed using WSxM 5.0 software.
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4

Atomic Force Microscopy of Amyloid Fibrils

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Aggregated samples from ThT experiments were diluted into MilliQ water (10-20 times) and deposited on freshly cleaved mica. After 10 min, the mica was rinsed with filtered Milli-Q water and dried under a gentle nitrogen stream. Images were recorded on an NTEGRA Prima setup (NT-MDT) using a goldcoated single crystal silicon cantilever (NT-MDT, NSG01, spring constant of ∼5.1 N/m) and a resonance frequency of ∼180 kHz. 512-pixel images were acquired with 0.5 Hz scan rate. Images were analyzed using the WSxM 5.0 software (Horcas et al. 2007) .
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5

Microparticle Characterization via AFM

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The synthesized microparticles
were analyzed and characterized using the atomic force microscope
(NT-MDT Solver Pro microscope, NT-MDT Spectrum Instruments, Zelenograd,
Moscow, RU), with a single-crystal silicon–antimony-doped probe
and a gold-coated base (NSG-01 from NT-MDT). To reduce nonlinearity
and hysteresis in the measurements, prior to the AFM analyses the
microscope was calibrated by a calibration grid (TGQ1 from NT-MDT).
The analyses were performed using the tapping mode where the cantilever
is driven to oscillate vertically near its resonance frequency. The
lyophilized sample was resuspended in Milli-Q water, deposited on
a mica substrate, and dried under a flux of argon. All the data were
collected using the software Nova (NT-MDT). The resolution of the
images acquired was 15 nm.
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6

Reversible Surface Wrinkles in PEDOT:PSS

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The reversible formation of surface wrinkles within the PEDOT:PSS thin films at different area strains was investigated using an atomic force microscope - AFM (NanoWizard 4 BioAFM, JPK Instruments AG, Germany) and a scanning electron microscope - SEM (Inspect F50, FEI, USA). The AFM images were taken with a cantilever probe (NSG01, NT-MDT, Russia) having a resonant frequency of around 150 kHz and a spring constant of 3.5 N/m. The SEM images were taken with an acceleration voltage of 2 kV.
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7

Multimodal Characterization of Purified Proteins

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Analysis of particle size by dynamic light scattering method was performed using a Zetasizer NanoS90 particle size analyzer (Malvern).
Atomic force microscopy was performed using an Integra Prima microscope and Nova SPM software (NT-MDT, Moscow, Russia). The scanning was performed in semi contact mode using gold cantilever NSG01 (NT-MDT).
Electron microscopy was performed on a JEM 1400 instrument (JEOL, Tokyo, Japan). Purified proteins were placed on carbon-formvar-coated copper grids (TED PELLA, Redding, CA, USA) and stained with 1% (w/v) uranyl acetate in methanol. The average size of the particles was determined using 10 particles.
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8

Quantitative Surface Characterization of Dried Films

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The surface structure of the dried films was characterized using a NanoWizard s 3 from JPK Instruments in quantitative imaging (QI) mode. A silicon probe (NSG01 from NT-MDT) with nominal spring constant of 5 N m À1 was used. Topography images were analysed using JPK Data Processing software, and the surface roughness (R a ) was calculated by averaging values from three different areas in the sample. Adobe Photoshop was used to quantify the surface coverage of particles of different sizes. The area covered by a certain population of particles was selected using the lasso tool and the pixels in the area were counted. The surface coverage was quantified by dividing the number of pixels occupied by the selected particle population by the total number of pixels in the image. This process was averaged for at least 3 areas in each of two representative regions of the sample. The centre, in a radius of up to 5.5 mm from the centre of the glass coverslip, and the edge, at a range of 5.5-9.0 mm from the centre of the coverslip. Within each specific region and sample, the overall morphology was very similar and therefore one representative image was chosen when comparing AFM topography maps.
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9

Atomic Force Microscopy of Protein Aggregates

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Samples from aggregation reactions were diluted into Milli-Q water (10–20 times; MilliporeSigma, Burlington, MA) and deposited on freshly cleaved mica. After 10 min, the mica was rinsed with filtered Milli-Q water (MilliporeSigma) and dried under a gentle nitrogen stream. Images were recorded on an NTEGRA Prima setup (NT-MDT, Moscow, Russia) using a gold-coated single crystal silicon cantilever (NT-MDT, NSG01, spring constant of ∼5.1 N/m) and a resonance frequency of ∼180 kHz. Here, 512 × 512-pixel images were acquired with a 0.5-Hz scan rate. Images were analyzed using the WSxM 5.0 software. For each sample, images were taken in at least three different 50 × 50-μm areas; the images shown in the figures are representatives for each sample. For the analysis of the oligomer sizes, flooding analysis was used; particles larger than 2 nm were included in the analysis.
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10

Electrochemical Characterization of TIECP Films

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The TIECP-coated electrode, counter electrode (Pt wire), and Ag/AgCl (Matsusada Precision, Japan) reference electrode were placed in a mixture solution including 20 μL sample (e.g., testosterone, urea, creatinine, 17β-estradiol and progesterone) and 20 mL 125 mM KCl, 5mM K4Fe(CN)6 and 5 mM K3Fe(CN)6 solution; the cyclic voltammetry of the electrochemical reactions was performed using a potentiostat (608-1A, CH Instruments, Inc., Austin, TX). The film thickness of the electroactive film can be directly quantitatively measured from the current density of the redox couple using the calibration curve between the current density and film thickness [41 (link),42 (link)]. The potential was scanned from −0.3 V to 0.8 V at a san rate of 0.1 V/s [43 (link),44 (link)] and the effects of target and interferent molecules (e.g., urea, creatinine, 17β-estradiol and progesterone) on the peak currents for the ferri-/ferrocyanide system were also recorded. TIECP films were freeze-dried before examination by a scanning electron microscope (Hitachi S4800, Hitachi High-Technologies Co., Tokyo, Japan), and atomic force microscopy (Solver P47H-PRO, NT-MDT Moscow, Russia) and a golden silicon cantilever (NSG01, NT-MDT).
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