The absorption spectra in this work were collected using a UV-2450 UV-vis spectrophotometer (Shimadzu, Japan). Dynamic light scattering (DLS) was measured using a Malvern Zetasizer Nano ZS90 (Malvern Instruments, Ltd., Worcestershire, UK). Transmission electron microscopy (TEM) was carried out using a JEM-2100 transmission electron microscope (JEOL, Japan) with a working voltage of 200 kV. The crystal structure was measured using a D 8 Advance X-ray diffractometer (Bruker, Germany). Circular dichroism measurements were collected using a MOS-500 circular dichroism spectrometer (Biologic, Germany). The concentration of cancer cells was determined by a TC10TM automated cell counter (Bio-Rad, USA). Flow cytometry measurements were obtained using a FACScan cytometer (Becton Dickinson, USA). The MTS assay was carried out using a Synergy 2 Multi-Mode Microplate Reader (Bio-Tek, USA). Cell fluorescence images were obtained using a confocal laser-scanning microscope (Olympus FV1000, Japan).
Mos 500 circular dichroism spectrometer
Manufactured by Bio-Logic
Sourced in France
The MOS-500 is a circular dichroism spectrometer manufactured by Bio-Logic. It is a laboratory instrument used to measure the differential absorption of left-handed and right-handed circularly polarized light by a sample. This information can be used to study the secondary structure and conformational changes of biomolecules, such as proteins and nucleic acids.
Automatically generated - may contain errors
Lab products found in correlation
Facscan cytometer, by BD (1 mentions)
Malvern zetasizer nano zs90, by Malvern Panalytical (1 mentions)
Tc10 automated cell counter, by Bio-Rad (1 mentions)
Uv 2450 uv vis spectrophotometer, by Shimadzu (1 mentions)
Synergy 2 multi mode microplate reader, by Agilent Technologies (1 mentions)
Fv1000, by Olympus (1 mentions)
D8 advance x ray diffractometer, by Bruker (1 mentions)
Jem 2100 transmission electron microscope, by JEOL (1 mentions)
Hemoglobin, by Sangon (1 mentions)
Guanidine hydrochloride, by Merck Group (1 mentions)
Ovalbumin (ova), by Merck Group (1 mentions)
Rf 5301pc fluorometer, by Shimadzu (1 mentions)
Zetaplus apparatus, by Brookhaven Instruments (1 mentions)
Tecnai g2 twin microscope, by Thermo Fisher Scientific (1 mentions)
Glutathione (gsh), by Sangon (1 mentions)
Hydrogen tetrachloroaurate 3, by Merck Group (1 mentions)
Bovine serum albumin (bsa), by Merck Group (1 mentions)
Human serum albumin (hsa), by Merck Group (1 mentions)
Uv 1800 spectrophotometer, by Shimadzu (1 mentions)
Rnase a, by Sangon (1 mentions)
8 protocols using mos 500 circular dichroism spectrometer
1
Multidisciplinary Characterization of Nanomaterials
2
CD Spectroscopy of TcMevK Protein
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Far-UV CD spectra were performed using an MOS-500 circular dichroism spectrometer (BioLogic, Grenoble, Isère, France) with standard procedures. TcMevK was diluted into 0.05 mg/mL with 50 mM phosphate buffer and transferred into a 1 cm quartz cell for incaution at 25 °C. After 5 min incubation, the CD spectra of TcMevK in the far-UV region that monitors the secondary structures of protein were detected from 190 nm to 250 nm. The thermal stability of TcMevK was determined using the 50 mM phosphate buffer (pH 8.0) from 20 °C to 90 °C. Furthermore, we investigated the stability of the TcMevK secondary structure over a pH range of 3.0 to 9.0. The mean residue ellipticities at 208 and 222 nm were utilized to characterize structural changes induced by temperature following baseline corrections.
3
Spectroscopic Characterization of Gold Nanoparticles
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Hydrogen
tetrachloroaurate(III) (≥99.9%), HSA, BSA, ovalbumin, lipase
and guanidine hydrochloride were purchased from Sigma. GSH, hemoglobin,
horseradish peroxidase, lysozyme, RNase A, carbonic anhydrase, immunoglobulin
G, trypsin, and BCA kit were purchased from Sangon Biotech. Phosphate
buffers (20 mM) with pH 4.0, 5.0, 6.0, 7.0, 8.0, and 9.0 were prepared
by mixing solutions of Na2HPO4 (20 mM) and NaH2PO4 (20 mM). The buffer pH was tuned by HCl/NaOH
solution.
Luminescence study was performed on a Shimadzu RF-5301PC
fluorometer. Time-resolved luminescence spectra were measured on an
Edinburgh FS 920 fluorometer. UV–vis spectra measurement was
performed on a Shimadzu UV-1800 spectrophotometer. TEM micrographs
were obtained by a FEI Tecnai G2-Twin microscope. XPS were obtained
using an ESCALAB-MKII spectrometer. CD spectra were carried out on
a Bio-Logic MOS 500 circular dichroism spectrometer. Secondary structural
contents were calculated by using the Dicro 2000 program. DLS and
ζ-potential measurement were performed on a Brookhaven ZetaPlus
apparatus.
tetrachloroaurate(III) (≥99.9%), HSA, BSA, ovalbumin, lipase
and guanidine hydrochloride were purchased from Sigma. GSH, hemoglobin,
horseradish peroxidase, lysozyme, RNase A, carbonic anhydrase, immunoglobulin
G, trypsin, and BCA kit were purchased from Sangon Biotech. Phosphate
buffers (20 mM) with pH 4.0, 5.0, 6.0, 7.0, 8.0, and 9.0 were prepared
by mixing solutions of Na2HPO4 (20 mM) and NaH2PO4 (20 mM). The buffer pH was tuned by HCl/NaOH
solution.
Luminescence study was performed on a Shimadzu RF-5301PC
fluorometer. Time-resolved luminescence spectra were measured on an
Edinburgh FS 920 fluorometer. UV–vis spectra measurement was
performed on a Shimadzu UV-1800 spectrophotometer. TEM micrographs
were obtained by a FEI Tecnai G2-Twin microscope. XPS were obtained
using an ESCALAB-MKII spectrometer. CD spectra were carried out on
a Bio-Logic MOS 500 circular dichroism spectrometer. Secondary structural
contents were calculated by using the Dicro 2000 program. DLS and
ζ-potential measurement were performed on a Brookhaven ZetaPlus
apparatus.
4
Circular Dichroism Analysis of Antimicrobial Peptides
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Secondary structure predictions were obtained using the Peptide Secondary Structure Prediction server, which predicts the secondary structure of peptides using a random forest classifier approach [19 (link)]. Circular Dichroism spectra were recorded on a MOS-500 Circular Dichroism Spectrometer (BioLogic, Seyssinet-Pariset, France) as previously described [38 (link)]. Full details are provided as Supplementary Materials . Figainin 2BN and picturin 1BN were dissolved in water at a concentration of 0.5 mg∙mL−1, and the solution was used to prepare samples containing TFE (25% and 50%), 20 mmol∙L−1 DPC and 10 mmol∙L−1 SDS at a 0.25 mg∙L−1 peptide concentration. Figainin 2BN was insoluble in 20 mmol∙L−1 SDS. Circular dichroism measurements are reported as mean residue molar ellipticity ([θ]MRE (deg∙cm2∙dmol−1)).
Peptide secondary structure was estimated using the online CD spectra deconvolution server Dichroweb [22 (link),23 (link),24 (link)]. The secondary structure content was determined through averaging the results obtained from CONTINLL [39 (link),40 (link)], CDSSTR [41 (link),42 (link)] and SELCON3 [43 (link),44 (link)] deconvolution programs. Peptide α-helical content was also calculated using the Forood formula: 100 × ([θ]222/max[θ]222) with max[θ]222 = − 40,000 [1 − (2.5/n)], where n = number of amino acid residues [25 (link)].
Peptide secondary structure was estimated using the online CD spectra deconvolution server Dichroweb [22 (link),23 (link),24 (link)]. The secondary structure content was determined through averaging the results obtained from CONTINLL [39 (link),40 (link)], CDSSTR [41 (link),42 (link)] and SELCON3 [43 (link),44 (link)] deconvolution programs. Peptide α-helical content was also calculated using the Forood formula: 100 × ([θ]222/max[θ]222) with max[θ]222 = − 40,000 [1 − (2.5/n)], where n = number of amino acid residues [25 (link)].
5
Circular Dichroism Spectroscopy of MDAP-2
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CD spectra were acquired at 25°C on a Bio-Logic MOS-500 circular dichroism spectrometer (FRA).
Scan parameters: the wavelength range was 190-270 nm, the acquisition duration was 1 s, the bandwidth was 2 nm, and the scanning speed was 100 nm/ min. Reaction system: PBS 5 mM (pH 7.4), 50% TFE (pH 7.4) solution, and 30% SDS (pH 7.4) solution. The concentration of MDAP-2 in the three solutions was 320 g/ml. A blank spectrum, a buffer solution lacking peptide, was also recorded and subtracted in the final analysis. Three spectra were accumulated and averaged to generate the final spectra. The mean residue ellipticity was calculated according to Wallace and Janes (Wallace and Janes 2001)
Scan parameters: the wavelength range was 190-270 nm, the acquisition duration was 1 s, the bandwidth was 2 nm, and the scanning speed was 100 nm/ min. Reaction system: PBS 5 mM (pH 7.4), 50% TFE (pH 7.4) solution, and 30% SDS (pH 7.4) solution. The concentration of MDAP-2 in the three solutions was 320 g/ml. A blank spectrum, a buffer solution lacking peptide, was also recorded and subtracted in the final analysis. Three spectra were accumulated and averaged to generate the final spectra. The mean residue ellipticity was calculated according to Wallace and Janes (Wallace and Janes 2001)
6
Circular Dichroism Spectroscopy of Protein Structures
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The CD spectra were obtained using a MOS-500 Circular Dichroism Spectrometer (Bio-Logic Science Instruments, Grenoble, France) according to the method of Greenfield[22] with some modifications. 350 µL sample solutions (0.1 mg/mL) were placed in quartz cuvettes with 0.1 cm path lengths. The measurements were recorded from 200 nm to 250 nm with a resolution of 1 nm. The structure content of α-helices, β-sheets, β-turns and unordered regions were calculated using the BeStSel software[23] (link), which can be accessed online at http://bestsel.elte.hu .
7
Characterization of PTX-loaded Protein Nanoparticles
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The PTX-loaded NPs were purified and analyzed using a size-exclusion chromatography (SEC) system (GE Healthcare) on a Superdex 200 10/300 GL column equilibrated with running buffer (50 mM NaH2PO4, 150 mM NaCl, pH 7.0). SEC analysis of protein before and after PTX encapsulation was monitored at 280 nm. The column was calibrated as previously described.40
Particle size and the morphology of HFtn-PTX, tLyP-1-HFtn-PTX and M-tLyP-1-HFtn-PTX NPs were examined by transmission electron microscopy (TEM) (JEM-1400, JOEL, Japan) using 2% uranyl acetate as the negative stain.
To examine whether the secondary structure would be changed due to the PTX encapsulation within the cage cavity, circular dichroism was performed to measure the secondary structure of samples by using MOS-500 circular dichroism spectrometer (Bio-Logic Science Instruments, France). The samples were dialyzed against phosphate buffer (50 mM NaH2PO4, pH 7.2) and the protein concentrations were determined by BCA (Novagen) and the samples were measured at the concentration of 0.14 μM.
Particle size and the morphology of HFtn-PTX, tLyP-1-HFtn-PTX and M-tLyP-1-HFtn-PTX NPs were examined by transmission electron microscopy (TEM) (JEM-1400, JOEL, Japan) using 2% uranyl acetate as the negative stain.
To examine whether the secondary structure would be changed due to the PTX encapsulation within the cage cavity, circular dichroism was performed to measure the secondary structure of samples by using MOS-500 circular dichroism spectrometer (Bio-Logic Science Instruments, France). The samples were dialyzed against phosphate buffer (50 mM NaH2PO4, pH 7.2) and the protein concentrations were determined by BCA (Novagen) and the samples were measured at the concentration of 0.14 μM.
8
Rb₁ Impacts on β-Glucosidase Structure
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To discover the effects of binding on the secondary structure of β‐glucosidase induced by Rb1, circular dichroism (CD) spectra (200–260 nm) of 10 μM β‐glucosidase were collected on a MOS‐500 Circular Dichroism Spectrometer (Bio‐Logic Science Instruments, Grenoble, France). The optimal concentrations of ginsenoside Rb1 were confirmed through the preliminary experiment which is 100 μM in 50 mM phosphate buffer at pH 7. In the presence or absence of ginsenoside Rb1, both samples were evaluated with a 1 mm cell, under constant nitrogen flush at 298 K. The scan rate was 200 nm × min−1, the response time was 1 s, and the bandwidth was 1 nm. The changes in the percentage of secondary structure elements of β‐glucosidase were computed by using CDNN software.
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