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Muscovite mica disc

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Muscovite mica discs are thin, transparent mineral sheets used as a substrate material in various scientific and industrial applications. They exhibit excellent insulating and dielectric properties, making them suitable for use in electronic components and devices.

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Lab products found in correlation

Scanasyst fluid, by Bruker (2 mentions) Nanoscope analysis version 2, by Bruker (2 mentions) Dimension icon afm, by Bruker (2 mentions) Scanasyst air, by Bruker (2 mentions) Poly l lysine solution, by Ted Pella (1 mentions) Origin 8, by OriginLab (1 mentions)

6 protocols using muscovite mica disc

1

Collagen Assembly on Mica Substrate

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The collagen (brand name: Purecol) was obtained from Advance Biomatrix Corporation. This collagen solution contains 3.1 mg/mL of collagen (purified bovine Type I (97%) and Type III collagen (3%)) at pH 2.0, and was diluted in a phosphate buffer containing 300 mM KCl, 10 mM Na2HPO4 at pH7.40. The initial collagen concentration was fixed at 12 μg/mL in all cases to exclude the possibility of collagen assembly in liquid crystalline phase, which is known to occur in tissues and at high collagen concentrations (>20 mg/mL)43 –45 (link). The collagen solutions at desired concentration (12 μg/mL) were then applied onto a freshly cleaved muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) and left for a 60-min incubation at pH 7.40, which was sufficiently long for collagen assembly onto the substrate.
Chien Y.C., Tao J., Saeki K., Chin A.F., Lau J.L., Chen C.L., Zuckermann R.N., Marshall S.J., Marshall G.W, & De Yoreo J.J. (2017). Using biomimetic polymers in place of noncollagenous proteins to achieve functional remineralization of dentin tissues. ACS biomaterials science & engineering, 3(12), 3469-3479.
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2

Dynamics of Nucleosome Array Adsorption

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The AFM samples were prepared using tetranucleosome array samples. A muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) was freshly cleaved and used as a supporting surface. Twenty microliters of poly-L-lysine solution (0.1% w/v, Mw 150,000-300,000, Ted Pella, Inc) was placed on the mica surface for 5 min and was then thoroughly rinsed with water and dried by a stream of nitrogen gas. After diluting nucleosome array to 30 nM in 20 mM HEPES buffer with 5 mM NaCl, 4 μL of the sample was deposited onto a poly-l-lysine pre-treated mica surface for a minute. The samples were prepared after 5 min, 75 min, 4 h, and 12 h incubation. The non-adsorbed nucleosome molecules were removed by washing with 50 microliter of background solution for 6 times. The samples were placed into an AFM equipped with a liquid cell. After the thermal relaxation for 10 min, the AFM images were collected at different locations of sample.
Zhang M., Díaz-Celis C., Liu J., Tao J., Ashby P.D., Bustamante C, & Ren G. (2024). Angle between DNA linker and nucleosome core particle regulates array compaction revealed by individual-particle cryo-electron tomography. Nature Communications, 15, 4395.
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3

Enamel Crystal Morphology Analysis

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A muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) was freshly cleaved and used as a supporting surface. The mica surface was washed with 50 µl poly-l-lysine solution (0.1% w/v, Ted Pella) for 5 min, thoroughly rinsed with water and dried by a stream of nitrogen gas. WT and MMP-20 null enamel crystals from the maturation and secretory stages were prepared as described in Fig. 1, and then dispersed in water by sonication for 10 min to prevent aggregation of the crystals. Three µl of this suspension was placed on the poly-l-lysine functionalized mica. To measure the thickness of the enamel crystals, all samples were imaged in air by a NanoScope 8 Atomic Force Microscope equipped with a J scanner. The images were captured in tapping mode with silicon tips (PPP-FMR rectangular cantilever, nominal spring constant k = 2 N/m, tip radius <10 nm, resonance frequency 75 kHz in air, Nanosensors™). Cantilevers were resonated at approximately 75 kHz with a free amplitude of 50 nm, and images were collected at a tapping amplitude of approximately 80% of free amplitude. All the width and thickness values were determined manually from the images using NanoScope Analysis 1.4 software and the histogram was plotted by Origin 8.5 (OriginLab Corporation).
Prajapati S., Tao J., Ruan Q., De Yoreo J.J, & Moradian-Oldak J. (2015). Matrix metalloproteinase-20 mediates dental enamel biomineralization by preventing protein occlusion inside apatite crystals. Biomaterials, 75, 260-270.
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4

AFM Imaging of Enamel Proteins

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All in-air and in-fluid AFM imaging were performed with a Dimension Icon AFM (Bruker, USA) in Peak Force Mode. The tips selected for in-air AFM imaging and in-fluid imaging were ScanAsyst-Air (k = 0.4 N/m, tip radius ~2 nm; resonance frequency 70 kHz in air) and ScanAsyst-Fluid+ (k = 0.7 N/m, tip radius ~2 nm; resonance frequency 150 kHz in air) (Bruker, https://www.brukerafmprobes.com/), respectively. Amel and Ambn were first mixed in Tris-HCl buffer solution (25 mM, 150 mM NaCl, pH 7.4), in which the concentration of Amel was fixed at 50 μg/mL and the concentrations of Ambn were adjusted to obtain various ratios including 1:10, 1:5, 1:3, 1:2, and 1:1 by weight. In addition, 50 μg/mL Amel alone and 25 μg/mL Ambn alone solutions were prepared. These protein solutions were dropped onto a freshly cleaved muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) and examined in fluid immediately using AFM.
A 50 μg/mL Amel solution in Tris-HCl buffer was dropped onto the mica disc for 5 min, rinsed with UPW, and then dried with argon. The same procedure was performed on 25 μg/mL Ambn, 17 μg/mL AB2, 17 μg/mL AB4, 17 μg/mL AmbnΔ5, 17 μg/mL AB2 and 50 μg/mL Amel, 17 μg/mL AB4 and 50 μg/mL Amel, and 17 μg/mL AmbnΔ5 and 50 μg/mL Amel. These samples were imaged in air using AFM. The images were analyzed using the image processing software package NanoScope Analysis version 2.0 (Bruker).
Shao C., Bapat R.A., Su J, & Moradian-Oldak J. (2022). Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin–Amelogenin Interactions. ACS biomaterials science & engineering, 9(4), 1834-1842.
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5

Adsorption of rP172-Enamelin Protein Complex

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The rP172 and enamelin 32 kDa were dissolved separately in pure water to yield final concentrations of 1000 and 300 μg/mL, respectively. The rP172 was diluted in a phosphate buffer containing 19 mM Na2HPO4 at pH 7.40. The final rP172 concentration was fixed at 50 μg/mL in all cases. Enamelin 32 kDa was introduced into rP172 solution at various final enamelin concentrations of 1 μg/mL (1:50), 2 μg/mL (2:50), 4 μg/mL (4:50), and 8 μg/mL (8:50). Then the mixed protein solutions were injected into liquid cells with a freshly cleaved muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) or highly oriented pyrolytic graphite (HOPG) (1010 mm, Ted Pella, Inc.) on the bottom, the solution was incubated in the liquid cell, and the adsorbed proteins were imaged by in situ AFM, with the nonadsorbed proteins flushed away by water after 50 min. The images were analyzed using the image processing software package SPIP 5.1.4 (Image Metrology A/S, Hørsholm, Denmark). The particle size distribution and areal coverage were calculated by the Particle and Pore Analysis module included in the SPIP 5.1.4 software.54 (link)
Tao J., Fijneman A., Wan J., Prajapati S., Mukherjee K., Fernandez-Martinez A., Moradian-Oldak J, & De Yoreo J.J. (2018). Control of Calcium Phosphate Nucleation and Transformation through Interactions of Enamelin and Amelogenin Exhibits the “Goldilocks Effect”. Crystal growth & design, 18(12), 7391-7400.
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6

AFM Imaging of Amelogenin and Ameloblastin Interactions

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All in-air and in-fluid AFM imaging were performed with a Dimension Icon AFM (Bruker, USA) in Peak Force Mode. The tips selected for in-air AFM imaging and in-fluid imaging were ScanAsyst-Air (k = 0.4 N/m, tip radius ~2 nm; resonance frequency 70 kHz in air) and ScanAsyst-Fluid + (k = 0.7 N/m, tip radius ~2 nm; resonance frequency 150 kHz in air) (Bruker, https://www.brukerafmprobes.com/), respectively. Amel and Ambn were first mixed in Tris-HCl buffer solution (25 mM, 150 mM NaCl, pH 7.4), in which the concentration of Amel was fixed at 50 μg/mL and the concentrations of Ambn were adjusted to obtain various ratios including 1:10, 1:5, 1:3, 1:2, and 1:1 by weight. In addition, 50 μg/mL Amel alone and 25 μg/mL Ambn alone solutions were prepared. These protein solutions were dropped onto a freshly cleaved muscovite mica disc (diameter 9.9 mm, Ted Pella, Inc.) and examined in fluid immediately using AFM.
A 50 μg/mL Amel solution in Tris-HCl buffer was dropped onto the mica disc for 5 min, rinsed with UPW, and then dried with argon. The same procedure was performed on 25 μg/mL Ambn, 17 μg/mL AB2, 17 μg/mL AB4, 17 μg/mL AmbnΔ5, 17 μg/mL AB2 and 50 μg/mL Amel, 17 μg/mL AB4 and 50 μg/mL Amel, and 17 μg/mL AmbnΔ5 and 50 μg/mL Amel. These samples were imaged in air using AFM. The images were analyzed using the image processing software package NanoScope Analysis version 2.0 (Bruker).
Shao C., Bapat R.A., Su J, & Moradian-Oldak J. (2023). Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin-Amelogenin Interactions. ACS biomaterials science & engineering, 9(4).
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