Mica surface

Manufactured by Agar Scientific

Sourced in Italy

Mica surfaces are thin, transparent sheets of a naturally occurring mineral known as mica. Mica is a versatile material that exhibits excellent electrical insulation and thermal properties. Mica surfaces are commonly used in various scientific and industrial applications as substrates or support materials for sample preparation and analysis.

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Lab products found in correlation

Nanowizard 3, by Bruker (4 mentions) Nchr silicon cantilever, by NanoWorld (3 mentions) Milli q water, by Merck Group (2 mentions) Nanodrop 2000, by Thermo Fisher Scientific (2 mentions) Axio observer d1, by Zeiss (2 mentions) Eclipse ti, by Nikon (2 mentions) Eclips ti, by Nikon (2 mentions) Gelred dye, by Biotium (1 mentions) Eclipse fluorescence spectrophotometer, by Agilent Technologies (1 mentions) Otespa r3 cantilevers, by Bruker (1 mentions) Ac240ts cantilevers, by Olympus (1 mentions) Cypher s afm, by Oxford Instruments (1 mentions) Nanoscope 5 controller, by Digital Instruments (1 mentions)

8 protocols using mica surface

DNA Origami Characterization Techniques

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The concentration of the DNA structures was inferred from the absorbance at a wavelength of 260 nm, measured using a low-volume UV-Vis spectrophotometer (Thermo Scientific, NanoDrop 2000). Concentrations obtained were typically ~10 nM for the DNA origami plates.
Steady-state donor and acceptor fluorescence emission spectra were obtained on a Cary Eclipse Fluorescence Spectrophotometer by excitation at 500 and 600 nm and detection in the wavelength range 530–600 and 635–700 nm, respectively.
Agarose gels were prepared at a gel percentage of 1 % and run at a voltage of 70 V for ~3 hours at 4 °C in an 11 mM MgCl₂ solution buffered with 0.5× TBE. The DNA structures were stained post-electrophoresis with GelRed dye (Biotium) for UV-transillumination. For reference, lanes with the p8064 scaffold and a 1 kb ladder containing linear fragments of different lengths were included in the gel (Supplementary Figure S1).
For AFM imaging, 5 μl of DNA origami sample was diluted to ~2 nM and deposited on a freshly cleaved mica surface (Agar Scientific). After an incubation period of 90 s, the surface was rinsed with Milli-Q water (Merck Millipore) and dried with nitrogen. Imaging was performed in air using a MFP-3D AFM System (Asylum, Oxford Instruments) in tapping mode. The resulting images were flattened and analysed using the software Gwyddion (see Supplementary Figure S2).

Hemmig E.A., Fitzgerald C., Maffeo C., Hecker L., Ochmann S.E., Aksimentiev A., Tinnefeld P, & Keyser U.F. (2018). Optical Voltage Sensing Using DNA Origami. Nano Letters, 18(3), 1962-1971.

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Characterizing Amyloid-Beta Fibrils with AFM

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The fibrils obtained from Aβ42 in presence and absence of CB[8] were recorded by AFM imaging (Agilent 5500 AFM) using tapping in air mode to further evaluate their morphology. Samples were prepared depositing a 10 μL drop solution after 6 days of incubation on a mica surface (Agar Scientific) approximately 0.5 cm × 1 cm. The surfaces had been previously cleaved in order to remove any extraneous organic matter. The solutions were allowed to remain on the freshly cleaved mica surfaces for 5 min before washing with mQ water (0.6 mL) and allowed to dry in air for at least 30 min. OTESPA-R3 cantilevers (Bruker AFM probes) with a resonant frequency of approx. 314 kHz, tip radius of 7 nm and spring constant 26 N m^–1 were used. Images were taken over an area of approximately 2 μm² at a rate of 1.02 lines per s with a resolution of 512 × 512 pixels. During measurements the topographic trace in both trace and retrace mode, amplitude and phase were all recorded.

Sonzini S., Stanyon H.F, & Scherman O.A. (2016). Decreasing amyloid toxicity through an increased rate of aggregation †Electronic supplementary information (ESI) available. See DOI: 10.1039/c6cp06765d. The data supporting the publication can be accessed at https://doi.org/10.17863/CAM.6653. Click here for additional data file.. Physical Chemistry Chemical Physics, 19(2), 1458-1465.

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Imaging DNA Origami Porin on Mica

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Five μL of the DNA origami
porin (10 nM) in 10 mM Tris-HCl, 1 mM EDTA, 20 mM MgCl₂, pH 8.0 was deposited on a freshly cleaved mica surface (Agar Scientific)
and incubated for 90 s. Subsequently, the surface was rinsed 3×
with 1 mL of Milli-Q water (Merck Millipore) to remove excess sample
and blow-dried with nitrogen. Imaging was carried out using a Cypher
S AFM (Oxford Instruments) in amplitude modulation in air and at room
temperature using AC240TS cantilevers (Olympus) with a nominal spring
constant of 2 N/m. The set-point to free amplitude ratio was generally
kept around 70% with a free oscillation amplitude of 20 nm. The frequency
of excitation was set close to the resonance of the first flexural
mode (around 70 kHz), and a repulsive mode was preferred. The scan
speed was set to either 1 or 2 Hz obtaining an image of 256 ×
256 pixels. The images were flattened and band-pass filtered using
Gwyddion (http://gwyddion.net/). Image analysis was performed
as described in the Supporting Information, Note S1, Figures S6, S7, and Tables S7, S8.

Göpfrich K., Li C.Y., Ricci M., Bhamidimarri S.P., Yoo J., Gyenes B., Ohmann A., Winterhalter M., Aksimentiev A, & Keyser U.F. (2016). Large-Conductance Transmembrane Porin Made from DNA Origami. ACS Nano, 10(9), 8207-8214.

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Atomic Force Microscopy Characterization

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AFM measurements were performed by using a Nanowizard III (JPK Instruments, Berlin, Germany) mounted on an Axio Observer D1 (Carl Zeiss, Berlin, Germany) or on an Eclipse Ti (Nikon, Tokyo, Japan) inverted optical microscope. Aliquots of protein solutions were deposited onto freshly cleaved mica surfaces (Agar Scientific, Assing S.P.A., Monterotondo, Roma, Italy) and incubated for up to 20 min before rinsing with deionized water and drying under a low-pressure nitrogen flow. Imaging of the protein was carried out in intermittent contact mode in air by using NCHR silicon cantilever (Nanoworld, Neuchâtel, Switzerland) with nominal spring constant ranging from 21 to 78 N/m and typical resonance frequency ranging from 250 to 390 kHz.

Guarrasi V., Rappa G.C., Costa M.A., Librizzi F., Raimondo M., Di Stefano V., Germanà M.A, & Vilasi S. (2021). Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein. Molecules, 26(8), 2371.

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Synthesis and Characterization of DODA-Keggin POM Hybrids

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A solution of DODA–Keggin POM hybrids was prepared by mixing DODA (1.58 × 10⁻⁶ mol·L⁻¹) and phosphotungstic anion (0.53 × 10⁻⁶ mol·L⁻¹) in absolute ethanol under magnetic stirring for 12 h. The molar ratio of 3:1 was kept for the DODA–Keggin POM hybrid solution in order to meet the charge balance between the POM anions (3 negative charges) and the DODA cation (1 positive charge). In the case of WD POM, the hybrid solution was prepared by mixing WD POM solution (0.26 × 10⁻⁶ mol·L⁻¹) and DODA (1.58 × 10⁻⁶ mol·L⁻¹) in ethanol under magnetic stirring for 12 h. In this case, the DODA/POM molar ratio was kept at 6:1 in order to meet the charge balance of WD, which bears 6 negative charges. Thin films of pure POM, pure DODA, and hybrid solutions were obtained by depositing a drop of each solution (about 9.5 µL) either on to freshly cleaved HOPG (ZYB grade, Bruker AFM probes) or mica surfaces (Agar scientific). The sample was allowed to dry under ambient conditions for more than 48 h before analysis. The DODA–POM hybrid films, after AFM imaging, were treated in an UV–ozone chamber (Jelight USA) for 10 min.

Raj G., Swalus C., Arendt E., Eloy P., Devillers M, & Gaigneaux E.M. (2014). Controlling the dispersion of supported polyoxometalate heterogeneous catalysts: impact of hybridization and the role of hydrophilicity–hydrophobicity balance and supramolecularity. Beilstein Journal of Nanotechnology, 5, 1749-1759.

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AFM Imaging of Protein Samples

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AFM measurements were performed by using a Nanowizard III (JPK Instruments, Germany) mounted on an Axio Observer D1 (Carl Zeiss, Germany) or on an Eclips Ti (Nikon, Japan) inverted optical microscope. Aliquots of protein solutions were deposited onto freshly cleaved mica surfaces (Agar Scientific, Assing, Italy) and incubated for up to 20 min before rinsing with deionized water and drying under a low pressure nitrogen flow. Imaging of the protein was carried out in intermittent contact mode in air by using NCHR silicon cantilever (Nanoworld, Switzerland) with nominal spring constant ranging from 21 to 78 N/m and typical resonance frequency ranging from 250 to 390 kHz.

Picone P., Vilasi S., Librizzi F., Contardi M., Nuzzo D., Caruana L., Baldassano S., Amato A., Mulè F., San Biagio P.L., Giacomazza D, & Di Carlo M. (2016). Biological and biophysics aspects of metformin-induced effects: cortex mitochondrial dysfunction and promotion of toxic amyloid pre-fibrillar aggregates. Aging (Albany NY), 8(8), 1718-1734.

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Imaging Amyloid-β Fibrillization Kinetics

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Aliquots of Aβ₄₀ samples with or without Hsp60, taken at the end of fibrillization kinetics, were deposited onto freshly cleaved mica surfaces (Agar Scientific, Assing, Italy) and incubated for up to 60 min at room temperature. Then, samples were rinsed with deionized water and dried under a low-pressure nitrogen flow. AFM measurements were performed using a Nanowizard III (JPK Instruments, Berlin, Germany) system mounted on an Eclipse Ti (Nikon, Japan) inverted optical microscope. Tapping mode AFM images were acquired in the air using a multimode scanning probe microscope driven by a nano-scope V controller (Digital Instruments, Bruker, Kennewick, WA, USA). Single-beam uncoated silicon cantilevers (type SPM Probe Mikromasch) were used. The drive frequency was between 260 and 325 kHz, and the scan rate was 0.25–0.7 Hz.

Caruso Bavisotto C., Provenzano A., Passantino R., Marino Gammazza A., Cappello F., San Biagio P.L, & Bulone D. (2023). Oligomeric State and Holding Activity of Hsp60. International Journal of Molecular Sciences, 24(9), 7847.

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Atomic Force Microscopy of Protein Samples

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Atomic force microscope (AFM) measurements were performed by using a Nanowizard III (JPK Instruments, Berlin, Germany) mounted on an Eclips Ti (Nikon, Tokyo, Japan) inverted optical microscope. Aliquots of protein solutions were deposited onto freshly cleaved mica surfaces (Agar Scientific, Assing S.P.A., Monterotondo, Roma, Italy) and incubated for up to 20 min before rinsing with deionised water and drying under a low-pressure nitrogen flow. Imaging of the protein was carried out in intermittent contact mode in air by using NCHR silicon cantilever (Nanoworld, Neuchatel, Switzerland) with nominal spring constant ranging from 21 to 78 N/m and typical resonance frequency ranging from 250 to 390 kHz.

Pizzo F., Mangione M.R., Librizzi F., Manno M., Martorana V., Noto R, & Vilasi S. (2022). The Possible Role of the Type I Chaperonins in Human Insulin Self-Association. Life, 12(3), 448.

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