All measurements were performed on an MOS-450 system (BioLogic, Claix, France) at a 4.0 nm bandwidth, 0.1 nm resolution, 0.1 cm path length, 4.0 s response time and 50 nm/min scanning speed. The individual N- and C-peptides as well as their equimolar mixtures were prepared in PBS (pH 7.4) at a final concentration of 10 μM and incubated at 37 °C for 30 min. Thermal denaturation was monitored by the ellipticity change at 222 nm by application of a thermal gradient from 15 °C to 90 °C with a 2 °C interval.
Mos 450 system
Manufactured by Bio-Logic
Sourced in France
The MOS-450 system is a laboratory equipment designed for the analysis and characterization of semiconductor materials. It provides essential data on the electrical properties of semiconductor samples, including carrier concentration, mobility, and resistivity. The MOS-450 system utilizes a measurement technique that allows for accurate and reliable data collection, making it a valuable tool for researchers and scientists working in the field of semiconductor technology.
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Lab products found in correlation
Ar2000ex system, by TA Instruments (1 mentions)
Monolith nt 115 system, by NanoTemper (1 mentions)
Escalab 250xi electron spectrometer, by Thermo Fisher Scientific (1 mentions)
Zetasizer nano z, by Malvern Panalytical (1 mentions)
D8 advance x ray diffractometer, by Bruker (1 mentions)
Uv 1700 spectrophotometer, by Shimadzu (1 mentions)
Talos f200, by Thermo Fisher Scientific (1 mentions)
Ir prestige 21 spectrometer, by Shimadzu (1 mentions)
9 protocols using mos 450 system
1
Thermal Denaturation of Peptide Mixtures
2
Absorption and Circular Dichroism Spectroscopy
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The tested samples were placed into a quartz spectrophotometer cell and measured by a BioLogic (MOS-450) system. Absorption spectra have been collected as HT voltage and converted into absorbance in a range of 180–300 nm. The resultant CD spectra were acquired after subtracting the solvent background.
3
Circular Dichroism Spectroscopy of Hydrogels
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Circular dichroism (CD) spectrum was obtained by a BioLogic (MOS-450) system. Hydrogel samples were placed in 0.1 cm quartz spectrophotometer cell (20-C/Q/0.1). The wavelength range varied from 190 to 280 nm. The acquisition period was 0.5 s and the step was 0.5 nm. The resultant CD spectrum was acquired after subtracting the solvent background.
4
Circular Dichroism Analysis of Peptide Interactions
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CD spectra were
acquired on a MOS-450 system (BioLogic, Claix, France) with the following
parameters: bandwidth, 4.0 nm; resolution, 0.1 nm; path length, 0.1
cm; response time, 4.0 s; and scanning speed, 50 nm/min. HR1P was
incubated with IIQ at 25 °C for 30 min in 10 mM phosphate buffer
(pH 7.4). N66 was incubated with IIQ at 30 °C for 30 min in 10
mM sodium acetate buffer (containing 10 mM sodium phosphate and 150
mM sodium chloride, pH 5.0). All samples were prepared with the buffer
solution at a final concentration of 10 μM and cooled to 25
°C for measurement. The CD data were presented as the mean residue
ellipticity. The α-helical content for these peptides was calculated
by assuming that 100% helicity corresponds to −33000 degrees
cm2 dmol–1. For the thermal unfolding
experiments, the CD absorbance was monitored at 222 nm with the temperature
for the peptide solutions ranging from 10 to 90 °C at a scan
speed of 2 °C/min. Samples at pH 5.0 contained 10 μM peptide
in 10 mM sodium acetate buffer (containing 10 mM sodium phosphate
and 150 mM sodium chloride). Samples at pH 7.4 contained 10 μM
peptide in 10 mM phosphate buffer.
acquired on a MOS-450 system (BioLogic, Claix, France) with the following
parameters: bandwidth, 4.0 nm; resolution, 0.1 nm; path length, 0.1
cm; response time, 4.0 s; and scanning speed, 50 nm/min. HR1P was
incubated with IIQ at 25 °C for 30 min in 10 mM phosphate buffer
(pH 7.4). N66 was incubated with IIQ at 30 °C for 30 min in 10
mM sodium acetate buffer (containing 10 mM sodium phosphate and 150
mM sodium chloride, pH 5.0). All samples were prepared with the buffer
solution at a final concentration of 10 μM and cooled to 25
°C for measurement. The CD data were presented as the mean residue
ellipticity. The α-helical content for these peptides was calculated
by assuming that 100% helicity corresponds to −33000 degrees
cm2 dmol–1. For the thermal unfolding
experiments, the CD absorbance was monitored at 222 nm with the temperature
for the peptide solutions ranging from 10 to 90 °C at a scan
speed of 2 °C/min. Samples at pH 5.0 contained 10 μM peptide
in 10 mM sodium acetate buffer (containing 10 mM sodium phosphate
and 150 mM sodium chloride). Samples at pH 7.4 contained 10 μM
peptide in 10 mM phosphate buffer.
5
Circular Dichroism Analysis of Peptides
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Lyophilized peptides were resuspended in ddH2O (pH 7.0) at a concentration of approximately 1 mg mL–1. All the HR-peptides and chimeric N-peptides were diluted in PBS (pH 7.4) to the specific final concentration indicated in the Results and discussion section. The peptides were incubated in a water bath set at 37 °C for 0.5 h before testing. CD spectra were acquired on an MOS-450 system (BioLogic, Claix, France) using the following parameters: band width, 4.0 nm; resolution, 0.1 nm; path length, 0.1 cm; response time, 4.0 s; and scanning speed, 50 nm min–1. For CD thermal denaturation analysis, the temperature was controlled by a BioLogic TCU250 system, and CD spectra were monitored at 222 nm from 10 °C to 90 °C at a scan speed of 2 °C min–1.
6
Circular Dichroism Spectroscopy of Samples
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The CD spectrum was obtained using a BioLogic (MOS-450) system. After subtracting the solvent background, all samples were loaded onto 0.1 cm quartz slides at 25 °C. The resultant CD spectrum was acquired by setting the conditions as follows: the wavelength ranged from 180 to 260 nm, the acquisition period was 0.5 s, and the step was 0.5 nm.
7
Peptide Hydrogel Synthesis and Characterization
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All peptides in the study were synthesized by standard solid‐phase peptide synthesis (SPPS), and purified by high performance liquid chromatography (HPLC). Hydrogels/formulas were prepared by heating–cooling method. Negative staining technique was used to observe the nanostructures of materials by using TEM (HITACHI HT7700 Exalens). CD spectrum were measured by a BioLogic (MOS‐450) system. Rheology test was carried out on an AR 2000ex system (TA instrument). The release behaviors of peptides was analyzed by liquid chromatograph (LC2020). Microscale thermophoresis and analysis of binding force was performed by using the Monolith NT.115 system (NanoTemper Technologies, Germany). All samples were tested at the temperature of 37 °C.
8
Circular Dichroism Spectroscopy of Hydrogels
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Circular dichroism (CD) spectra were obtained using a BioLogic (MOS-450) system. Hydrogel samples were placed in a 0.1 cm quartz spectrophotometer cell (20-C/Q/0.1). The wavelength range was from 190 to 280 nm. The acquisition period was 0.5 s and the step size was 0.5 nm. The resultant CD spectrum was acquired after subtracting the solvent background.
9
Comprehensive Characterization of BSA-Ce6@IrO2/MnO2 Nanoparticles
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The morphology of the BSA-Ce6@IrO2/MnO2 nanoparticles was characterized using high-resolution transmission electron microscopy (HR-TEM, Talos F200S, FEI, Hillsborough, OR, USA) equipped with an energy dispersive spectroscopy (EDS) attachment. Fourier transform infrared (FT-IR) spectra were recorded on a IRPrestige-21 spectrometer (Shimadzu, Kyoto, Japan). X-ray photoelectron spectra (XPS) were collected with an EscaLab 250Xi electron spectrometer (ThermoFisher, Waltham, MA, USA). Powder X-ray diffraction (XRD) patterns were obtained on a D8 ADVANCE X-ray diffractometer (Bruker, Billerica, MA, USA) supplied with Cu Kα radiation (λ = 1.5418 Å) at 40 kV and 40 mA. UV-Vis-NIR absorbance spectra were recorded on a UV-1700 spectrophotometer (Shimadzu, Kyoto, Japan). Concentrations of Mn and Ir were detected by inductively coupled plasma optical emission spectroscopy (ICP-OES, Prodigy7, Leeman Laboratories, Hudson, NH, USA). Prior to measurements samples were digested in aqua regia. Dynamic light scattering (DLS) and zeta potential measurements were performed with a Zetasizer Nano-ZS (Malvern Instruments, Malvern, UK). Circular dichroism spectra were measured using a MOS-450 system (BioLogic, Seyssinet-Pariset, France).
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