Bioatr 2 unit

Manufactured by Bruker

Sourced in Germany

The BioATR II unit is a piece of lab equipment designed for attenuated total reflection (ATR) infrared spectroscopy. It is used for the analysis of biological samples and materials.

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Lab products found in correlation

Tensor 2, by Bruker (2 mentions) J 715, by Jasco (1 mentions) Vertex 70 spectrometer, by Bruker (1 mentions) Haake dc30 k20, by Thermo Fisher Scientific (1 mentions) Opus 7, by Bruker (1 mentions) Tensor 27, by Bruker (1 mentions) Opus 6.5 software package, by Bruker (1 mentions) Vertex 70 ftir spectrometer, by Bruker (1 mentions)

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BioATR-II (8 citations)

8 protocols using bioatr 2 unit

FTIR Analysis of Analyte-AuNP Interactions

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Infrared spectroscopic
studies were performed using a Vertex 70 FTIR spectrometer (Bruker
Optics, Ettlingen, Germany) equipped with a BioATRII unit (Bruker
Optics, Ettlingen, Germany). The ATR crystal surface interfacing with
the sample was made from a circular section of a silicon wafer providing
8–10 internal reflections. In between and prior to any measurement,
the surface of the ATR crystal was cleaned with water, acetone, methanol,
and again water to avoid any cross-contamination. For the actual sample
measurements, the Si ATR waveguide was covered with 20 μL of
neat analyte solution or a mixture (1:1) of 10 μL of AuNPs and
10 μL of the analyte, which was a 40 ppm CV stock solution.
Every 100 s, an IR spectrum was recorded during evaporation of the
solvent until the sample was completely dried (i.e., approx. 2.5–3
h). Every spectrum represents the average of 100 spectral scans in
the region of 4000–500 cm^–1 at a spectral
resolution of 2 cm^–1. For comparison measurements,
10 μL of a 40 ppm crystal violet was mixed at 1:1 with 10 μL
of Millipore water. For better comparison, all spectra were baseline-corrected.

Repp S., Lopez-Lorente Á.I., Mizaikoff B, & Streb C. (2020). Hybrid Gold Nanoparticle–Polyoxovanadate Matrices: A Novel Surface Enhanced Raman/Surface Enhanced Infrared Spectroscopy Substrate. ACS Omega, 5(39), 25036-25041.

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FTIR Analysis of CRES Protein Samples

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Mid- and high concentration CRES samples, 6.4 mg/ml and 15 mg/ml, respectively, in 4 mM potassium phosphate buffer, pH 7.4 were incubated for 2 weeks at 4 °C. An aliquot was removed from each and diluted to 0.17–0.21 mg/ml with 4 mM potassium phosphate buffer, pH 7.4. Infrared spectra were obtained at a resolution of 4 cm⁻¹ using a FTIR spectrometer equipped with a BioATRII unit for measurement of liquid samples (Bruker Optics, Billerica, MA). Absorbance band maxima were determined from the minima in the second derivative which was determined using the Grace software http://plasma-gate.weizmann.ac.il/Grace/.

Do H.Q., Hewetson A., Myers C., Khan N.H., Hastert M.C., M. Harsini F., Latham M.P., Wylie B.J., Sutton R.B, & Cornwall G.A. (2019). The Functional Mammalian CRES (Cystatin-Related Epididymal Spermatogenic) Amyloid is Antiparallel β-Sheet Rich and Forms a Metastable Oligomer During Assembly. Scientific Reports, 9, 9210.

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FTIR Spectroscopy of Peptide Samples

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All FTIR spectra were collected using a Tensor-37 series FTIR spectrophotometer with a BioATR II unit (Bruker Optics, UK) as the sampling platform with a photovoltaic mercury cadmium telluride (MCT) detector and a Bruker Optics workstation, which was equipped with OPUS software. Low volume (20 μL) peptide samples (100 μM) were placed in a circular sampling area of radius 2 mm with a pathlength of 6 μm. The temperature of the sample was maintained at 20 °C by means of flow connectors to a circulating water bath. All FTIR spectra were collected between 4000 and 850 cm⁻¹ with a resolution of 4 cm⁻¹, scanner velocity 20 kHz, 128 scans, phase resolution 32 and zero filling factor 4.

De Santis E., Alkassem H., Lamarre B., Faruqui N., Bella A., Noble J.E., Micale N., Ray S., Burns J.R., Yon A.R., Hoogenboom B.W, & Ryadnov M.G. (2017). Antimicrobial peptide capsids of de novo design. Nature Communications, 8, 2263.

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Peptide Conformational Analysis via FTIR and CD

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Peptides with different concentrations (1000, 500, 200, 100, and 50 μM) were prepared in water, and analysis was performed immediately. For [AA], [WW], and [II] groups, equal volumes of charged peptides were mixed (as a total of 20 μl) and put directly into FTIR stage. Analysis was performed with Bruker Tensor II with BioATR II unit. For background spectrum, water was measured first, and then peptides in water were subtracted automatically in the device. Analysis was performed between 1800 and 900 cm⁻¹, with 4-cm⁻¹ resolution and 60 scans. For CD measurements, analysis was performed in water with a concentration of 200, 100, and 50 μM for co-assembled peptides and 200 μM for individual peptides with a volume of 1 ml. Jasco J-715 was used to collect spectra from 190 to 400 nm, with 0.1-nm data pitch and bandwidth arranged as 1.0 nm.

Hamsici S., White A.D, & Acar H. (2022). Peptide framework for screening the effects of amino acids on assembly. Science Advances, 8(3), eabj0305.

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ATR-FTIR Analysis of Calmodulin Mutants

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Attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) was performed on a Bruker Vertex 70 spectrometer equipped with a BioATR II unit and a liquid nitrogen-cooled mercury cadmium telluride (MCT) detector. The following protein concentrations were used: CaM92AzF:6.3 mM/CaM92AzF+P1:1.2 mM/CaM92AzF+P2:1.2 mM/CaM92AzF+P3:0.5 mM/CaM92AzF+P4:1.2 mM/CaM108AzF:4.1 mM/CaM108AzF+P1:2.6 mM/CaM108AzF+P2:1.5 mM/CaM108AzF+P3:2.9 mM/CaM108AzF+P4:1.6 mM. The data were collected from 800 to 3800 cm⁻¹ with a resolution of 2 cm⁻¹ averaging 64 scans. For further data analysis of the spectral region between 2000 and 2200 cm⁻¹, OriginPro 2016 was used. All curves were smoothed by Savitzky-Golay interpolation (over 30 points and with second-order polynomials). A baseline correction was performed with a polynomial fit of the fifth order to subtract the slowly varying background below the azido stretching band (Table II). All spectra were normalized to unity to compensate for concentration differences.

Creon A., Josts I., Niebling S., Huse N, & Tidow H. (2018). Conformation-specific detection of calmodulin binding using the unnatural amino acid p-azido-phenylalanine (AzF) as an IR-sensor. Structural Dynamics, 5(6), 064701.

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FTIR Analysis of Charged Peptides

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Peptides (KFFIIK and EFFIIE) with a concentration of 300 μM were prepared in water, and analysis was performed immediately. For the peptide combination [II], equal volumes of charged peptides were mixed (as a total of 20 μl) and put directly into the FTIR stage. Analysis was performed with Bruker Tensor II with BioATR II unit. For the background spectrum, water was measured first, and then peptide groups were subtracted automatically in the device. Analysis was performed between 1800 and 900 cm⁻¹, with 4 cm⁻¹ resolution and 60 scans.

Hamsici S., Gunay G, & Acar H. (2022). Controllable membrane damage by tunable peptide aggregation with albumin. AIChE journal. American Institute of Chemical Engineers, 68(12), e17893.

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Characterizing Cuticular Wax Melting Profiles

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Infrared spectra of cuticular waxes were obtained with a Fourier transform infrared spectrometer (Bruker Tensor 27) in horizontal attenuated total reflection (ATR) mode using the BIO-ATR II unit (Bruker) equipped with a zinc selenide crystal. The extracted cuticular waxes were applied to the crystal as a solution of trichloromethane (Roth). After evaporation of the organic solvent at 90°C, the temperature was adjusted at 20°C by a stainless-steel envelope as part of the BIO-ATR II unit and a custom-made sample holder connected to the water circuit of a thermostat (Thermo Scientific Haake DC30-K20). Infrared spectra were scanned in a wavenumber range from 4000 cm -1 to 670 cm -1 . The resolution was set to 2 cm -1 with an acquisition time of 120 scans. The BIO-ATR II unit was continuously purged with dry, carbon dioxide-free air (K-MT-LAB 3, Parker Hannifin). The OPUS 7 (Bruker) software was used to analyse the spectra.
For melting curve analysis of cuticular waxes, infrared spectra were recorded from 20°C to 92°C using the asymmetric stretching vibration of methylene groups between 2916 cm -1 and 2924 cm -1 . The initial temperature was set to 20°C and, then, raised at temperature intervals of 4°C to 44°C and in 1°C steps to 92°C.

Diarte C., Xavier de Souza A., Staiger S., Deininger A.C., Bueno A., Burghardt M., Graell J., Riederer M., Lara I, & Leide J. (2021). Compositional, structural and functional cuticle analysis of Prunus laurocerasus L. sheds light on cuticular barrier plasticity. Plant physiology and biochemistry : PPB, 158.

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Infrared Spectroscopy and SEM Analysis

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Infrared spectroscopic studies were performed using a Vertex 70 FTIR spectrometer (Bruker Optics, Ettlingen, Germany) equipped with a BioATRII unit (Bruker Optics, Ettlingen, Germany). The ATR crystal surface interfacing with the sample was made from a circular section of a silicon wafer providing 8e10 internal reflections. IR radiation is coupled into this silicon ATR plate via a secondary zinc selenide (ZnSe) ATR crystal providing a hemispherical shape for efficient coupling of radiation from the FTIR spectrometer into the Si ATR waveguide. A liquid nitrogen cooled mercu-ryÀcadmiumÀtelluride (MCT) detector (Bruker Optics, Ettlingen, Germany) was used for signal recording. Data acquisition and processing was performed using the OPUS 6.5 software package (Bruker Optics, Germany), and the Essential FTIR spectroscopy toolbox (Operant LLC, USA).
Scanning electron microscopy (SEM) images were acquired using a Helios Nanolab 600 scanning electron microscope (FEI Corp., Eindhoven, the Netherlands). The Au concentration was obtained via inductively coupled e atomic emission spectrometry (ICP-AES) using an Ultima 2 system (HORIBA Jobin Yvon, Tokyo, Japan).

Bibikova O., Haas J., López-Lorente Á.I., Popov A., Kinnunen M., Ryabchikov Y., Kabashin A., Meglinski I, & Mizaikoff B. (2017). Surface enhanced infrared absorption spectroscopy based on gold nanostars and spherical nanoparticles. Analytica chimica acta, 990.

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