The synthesized conjugates (20 µg mL−1) were tested with UV-vis spectroscopy in a 1 cm quartz cell by using Shimadzu UV-2600 spectrometer. Then the fluorescent emission spectra of the same samples were recorded by Horiba Jobin Yvon Fluorolog-3 with slit width 5 nm for both excitation and emission. The solid FTIR study was performed on a PerkinElmer FTIR (Frontier) spectrometer using the attenuated total reflection (ATR) technique which uses the ATR prism alone as the background. The matrix-assisted laser desorption ionization time of flight (MALDI-TOF) was measured by a Bruker autoflex speed spectrometer. Transmission electron microscopic (TEM) studies were conducted with the JEOL 1200X TEM and atomic force microscopic (AFM) studies were done by an Agilent 5420 atomic force microscope using the tapping mode. Each characterization study was repeated with different batches of C-dots-conjugates to verify the consistency of the data and the stability of the complexes.
Autoflex speed spectrometer
Manufactured by Bruker
Sourced in France, Germany
The Autoflex Speed spectrometer is a laboratory instrument designed for high-performance mass spectrometry analysis. It provides accurate and reliable measurements of molecular weights and structures of a wide range of analytes, including small molecules, peptides, and proteins.
Automatically generated - may contain errors
Lab products found in correlation
Uv 2600 spectrometer, by Shimadzu (2 mentions)
5420 atomic force microscope, by Agilent Technologies (1 mentions)
Ftir frontier spectrometer, by PerkinElmer (1 mentions)
J 1500 circular dichroism spectrometer, by Jasco (1 mentions)
Unity inova 300 spectrometer, by Agilent Technologies (1 mentions)
Fluoromax 4 spectrofluorometer, by Horiba (1 mentions)
Cary 100 bio uv vis spectrophotometer, by Agilent Technologies (1 mentions)
J 815 spectrometer, by Jasco (1 mentions)
Proteomics grade trypsin, by Agilent Technologies (1 mentions)
Optilab dsp interferometric refractometer, by Wyatt Technology (1 mentions)
500 mhz spectrometer, by Agilent Technologies (1 mentions)
Mercury spectrometer, by Agilent Technologies (1 mentions)
Mtp384 polished steel target, by Bruker (1 mentions)
Protein calibration standard 1, by Bruker (1 mentions)
10 protocols using autoflex speed spectrometer
1
Characterization of C-dots Conjugates
2
Comprehensive Biophysical Characterization Techniques
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1H NMR spectra were collected on a Varian Unity INOVA-300 spectrometer with TMS as the internal standard. 13C NMR spectra were recorded on a Varian Unity INOVA-300 spectrometer at 75 MHz. MALDI-TOF measurements were recorded on a Bruker Autoflex Speed spectrometer with DCTB as the matrix. UV–Vis spectra were recorded on a UV-1800 Shimadzu spectrometer. CD measurements were performed on a Jasco J-1500 circular dichroism spectrometer, equipped with a PFD-425S/15 Peltier-type temperature controller. Solution excitation and steady-state fluorescence emission spectra were recorded on a FluoroMax-4 spectrofluorometer (Horiba Scientific) and analyzed with an Origin (v8.0) integrated software FluoroEssence (v2.2). TEM images were performed on a Tecnai G2 Spirit BioTWIN electron microscope (acceleration voltage: 120 kV). Electron paramagnetic resonance (EPR) measurements were performed on a JEOL JES-FA200 apparatus, with the utilization of 2,2,6,6-tetra-methylpiperidine as the spin trap for 1O2. Fluorescence microscopy images were performed on an inverted fluorescence microscope (Olympus IX81).
3
Oligonucleotide Characterization by HPLC, MS, and CD
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All chemicals and solvents were of laboratory grade as obtained from commercial suppliers and were used without further purification. Reversed‐phase HPLC was carried out by using a HITACHI 655A‐12 liquid chromatograph connected to L6200A intelligent pump and 655A variable‐wavelength UV monitor with a 4×250 mm RP‐18 (10 μm) LiChrospher 100 column. The molecular masses of the oligonucleotides were determined by MALDI‐TOF MS on a Bruker Autoflex Speed spectrometer in linear positive mode with 3‐hydroxypicolinic acid as matrix. The thermal melting curves were measured with an Agilent Technologies Cary 100 Bio UV‐vis spectrophotometer equipped with a thermoelectric controller. The temperature was measured continuously in the reference cell using a Pt‐100 resistor at a heating rate of 1 °C min−1. The Tm values were determined from the melting curves using the software Meltwin (version 3.0).[25] CD spectra were recorded at 25 °C on a Jasco J‐815 spectrometer.
4
Characterization of C-dot-trans-chalcone Conjugates
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The conjugates (20 μg/mL) were characterized by UV-Vis spectroscopy in a 1 cm quartz cell using Shimadzu UV-2600 spectrometer. The fluorescent emission spectra of the C-dots-trans-chalcone conjugates and the free chalcone were obtained by Horiba Jobin Yvon Fluorolog-3 with slit width 5 nm for both excitation and emission. The molecular weights of each C-dot-trans-chalcone derivative was analyzed with a Matrix-Assisted Laser Desorption/Ionization-Time of Flight (MALDI-TOF) mass spectrometer using a Bruker auto flex speed spectrometer.
5
Protein Identification Using MALDI-TOF-MS
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Protein bands were cut from PAS-stained gel. Separated bands were washed several times with acetonitrile and water and digested overnight at room temperature into peptides using in-gel digestion with proteomics grade trypsin (Agilent Technologies). The peptides were extracted from the gel using acetonitrile. A matrix-assisted laser desorption/ionization time-of-flight spectrometry (MALDI-TOF-MS) on a Bruker Autoflex Speed spectrometer (Bruker Daltonics, Wissembourg, France) was used to identify the protein bands. The mass spectrometer was calibrated externally using Bovine serum albumin tryptic peptides. Peptide mixture (1 μL) was co-crystallized onto the anchorchip MALDI-TOF target plate with an equal amount of matrix solution (0.3 mg/mL of α-cyano-4-hydroxycinnamic acid in acetone and ethanol in 1:2 volume ratio and 0.1% trifluoroacetic acid). Mascot software was used for protein identification using peptide mass fingerprinting. Searches were performed against all available sequences in public databases.
6
Characterization of Polymer Samples
7
MALDI-TOF-MS Analysis of CAEE
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The CAEE was mixed with the matrix solvent 2,5-dihydroxybenzoic acid (DHB), prepared by dissolving in methanol (10 mg mL−1) with 0.1% TFA. The sample was prepared at a ratio of 1 : 6 (matrix : CAEE), which meant 1 μL of matrix solution was added to 6 μL of analyte solution (CAEE). MALDI-TOF-MS analysis was performed on a Bruker Autoflex Speed spectrometer at an accelerating voltage of 19 kV (per spectrum around 2000 laser shots). The sample with the matrix solution was placed over a stainless-steel plate and dried before being subjected to the analysis. The spectrum reproducibility was checked by taking measurements at five different spots on the sample.
8
Comprehensive Characterization of Materials
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Two-point probe current–voltage
(I−V) measurements
were performed
using an Agilent 4155C semiconductor analyzer. Absorption spectra
were measured by using a PerkinElmer Lambda 900 or a Lambda 1050 spectrometer.
Cyclic voltammetry measurements were performed inside a nitrogen-filled
glovebox using an Autolab PGSTAT30 potentiostat. A 0.1 M solution
of tetrabutylammonium hexafluorophosphate in dichloromethane
was used as the electrolyte. Potentials are reported versus Ag/AgCl. 1H NMR (400 MHz) and 13C NMR (100 MHz) spectra were
recorded on a Varian Mercury spectrometer. Chemical shifts are given
in ppm and referenced to the deuterated solvent residual peak. Matrix-assisted
laser desorption ionization time-of-flight (MALDI-TOF) mass spectroscopy
was recorded on a Bruker Autoflex Speed spectrometer by using α-cyano-4-hydroxycinnamic
(CHCA) acid as matrix.
(I−V) measurements
were performed
using an Agilent 4155C semiconductor analyzer. Absorption spectra
were measured by using a PerkinElmer Lambda 900 or a Lambda 1050 spectrometer.
Cyclic voltammetry measurements were performed inside a nitrogen-filled
glovebox using an Autolab PGSTAT30 potentiostat. A 0.1 M solution
of tetrabutylammonium hexafluorophosphate in dichloromethane
was used as the electrolyte. Potentials are reported versus Ag/AgCl. 1H NMR (400 MHz) and 13C NMR (100 MHz) spectra were
recorded on a Varian Mercury spectrometer. Chemical shifts are given
in ppm and referenced to the deuterated solvent residual peak. Matrix-assisted
laser desorption ionization time-of-flight (MALDI-TOF) mass spectroscopy
was recorded on a Bruker Autoflex Speed spectrometer by using α-cyano-4-hydroxycinnamic
(CHCA) acid as matrix.
9
Anhydrous Reaction Conditions and Characterization
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All chemical reactions were carried out in oven-dried glassware under anhydrous conditions with freshly distilled solvents under a positive pressure of argon gas, and all chemicals purchased were reagent grade and used without further purification, unless otherwise noted. Chemical reactions were monitored by thin-layer chromatography (TLC). Spots were visualized by UV light (254 nm) and charring with a solution of 10% sulphuric acid in MeOH. Column chromatography was performed on silica gel (200-300 mesh). were performed on an AccuTOF-ESI mass spectrometer. MALDI-TOF mass spectra were performed on a Bruker Autoflex Speed spectrometer using trihydroxyacetophenone as the matrix, unless otherwise noted.
10
MALDI-TOF Protein Analysis Protocol
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A Bruker Autoflex Speed spectrometer (Bruker Daltonics GmbH, Bremen, Germany) was used. Samples were dissolved in MilliQ water at 1% of protein concentration and then diluted 1 : 100. One μL was loaded on a Bruker MTP 384 Polished Steel target and 1 μL of sinapinic acid in 1% formic acid/50% ACN (Bruker Daltonics, Billerica, MA, USA) was used as matrix. Ions were detected in positive linear mode at a mass range of m/z 5-25 kDa. For calibration, 0.5 μL of Protein Calibration Standard I (Bruker Daltonics) was loaded on the target with 0.5 μL, of sinapinic acid solution.
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