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Dts software

Manufactured by Malvern Panalytical
Sourced in United Kingdom

DTS software is a data analysis and visualization tool for thermal analysis data from Malvern Panalytical's thermal analysis instruments. It allows users to view, process, and analyze thermal data in a streamlined and efficient manner.

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35 protocols using dts software

1

DLS Characterization of Purified Proteins

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DLS experiments were performed at 20°C on a Zetasizer Nano ZS instrument (Malvern Instrument) controlled by DTS software (version 5.1, Malvern Instruments Ltd). The instrument has a 90° scattering angle. The purified protein, at a concentration of 100 μM in a resuspension buffer at pH 8 containing 10 mM CHAPS, was filtered through 20 nm filters into a 40 μl cuvette. A single measurement consisted of 20 runs of 12 s each. All measurements were done in triplicate. The samples gave a clear signal (the y-intercept was 0.95) and required only moderate attenuation (set at 7).
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2

Particle Size and Surface Charge Analysis

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Particle sizes and surface charges were determined by dynamic light scattering and laser doppler, respectively, using a Zetasizer Nano and analyzed using Data Transfer Assistance (DTS) software (Malvern Instrument, Malvern, UK) [28 (link)].
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3

Nanoparticle Characterization by PCS

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SALN size and polydispersity index (PDI) were determined by photon correlation spectroscopy (PCS) technique using a Zetasizer Nano ZS analyser system (Zetasizer version 6.12; Malvern Instruments, Worcs, UK). The results were expressed as the average of three different measurements.
Particle surface charge (Z-Potential value) was measured by using the same apparatus, equipped with a 4 mW He–Ne laser (633 nm) and DTS software (Version 5.0, Malvern Instruments, Worcs, UK). Measurements were performed in triplicate and each measurement was averaged over at least 12 runs.
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4

Dynamic Light Scattering Analysis of MBP Proteins

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The Nano-S Dynamic Light Scattering system (Malvern Instruments Ltd, Malvern, UK) equipped with a 633 nm laser and a fixed scattering angle (173°) was employed to analyze purity of MBP and MBP-netrin-4 delta protein as described previously [11 (link), 12 (link)]. Traditional DLS analysis provides the translational diffusion coefficient that was converted to Stokes radius or hydrodynamic radius via the Stokes−Einstein relationship using the DTS software (Malvern Instruments Ltd., Malvern, UK) supplied with the instrument. Both proteins were allowed to equilibrate for 4 min at 20°C prior to DLS measurements, after which multiple records of the DLS profile were collected for data analysis. Purity of MBP-netrin-4 delta (delta: missing the C-terminal NTR domain) was studied over the range of concentrations from 3.28 to 1.7 mg/ml whereas MBP alone was studied from 1.80 to 1.0 mg/ml in 1 x TBS buffer.
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5

Dynamic Light Scattering Characterization

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Dynamic light scattering (DLS) was performed on a Malvern Zetasizer Nano ZS with a HeNe laser at 633 nm. Temperature scans and size measurements were carried out at a fixed scattering angle of 173° (back scatter). Temperature scans were run from 4°C to 90°C at a rate of 2°C/min. Purified protein preparations were diluted to 1 mg/ml (22 μM) in the indicated buffers and additives. Data analysis was performed on intensity and volume size distribution curves and the molecular mass and Z-average size was calculated using Malvern DTS software. The intensity size distribution, the first order result, is weighted according to scattered intensity of each particle fraction whereas the volume size distribution represents the relative proportion based on the mass or volume, which is derived from the intensity size distribution via the Mie theory. The Z-average provides a reliable measure of the mean size of the particle size distribution [33 (link)].
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6

Hydrodynamic Radius of α-Synuclein

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DLS was performed on a Malvern Zetasizer Nano operating at a laser wavelength of 633 nm at 25 °C in 3 × 3 mm cuvettes and with 50 μM of methionine-oxidized, N-terminally acetylated α-Syn in NMR buffer. Hydrodynamic radii were calculated based on volume-weighted analyses of scattered light, using the Malvern DTS software.
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7

Physiochemical Characterization of AmB-PGA Nanoparticles

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The zeta potential gives an indication of the charge acquired by a particulate system on its suspension in aqueous medium. The zeta potential of the nanoparticles was determined using DTS software (Malvern Instruments Limited, Malvern, UK) based on M3-PALS technology. The concentration of the AmB–PGA formulation used was 10−4 M. Particle size was determined by photon correlation spectroscopy (90Plus/BI-MAS, Brookhaven Instruments, Holtville, NY, USA). Samples were filtered using a 0.22 μm syringe filter (polyethersulfone, Millipore) to remove contamination with dust particles. Dynamic light scattering measurements were carried out using DynaPro-TC-04 equipment (Protein Solutions, Wyatt Technology, Santa Barbara, CA, USA) equipped with a temperature-controlled microsampler. The size and surface morphology of the AmB-loaded nanoparticles were characterized using an electron microscope (CM-10, Philips, Hamburg, Germany). For transmission electron microscopy studies, the AmB–PGA formulation was used at a concentration of 10 μg/mL AmB equivalents in double-distilled water. The details of these procedures are provided in the Supplementary materials section.
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8

Characterization of Transfection Complexes

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The particle size and zeta potential of transfection complexes were measured using Dynamic Light Scattering (DLS) and Laser Doppler Velocimetry (LDV), respectively by a Malvern NanoZS instrument and DTS software (Malvern Instruments, UK). Various amounts of PPI or modified PPIs in HBG buffer were added to a final DNA concentration of 5 μg/ml. The mixture was incubated for 20 min at room temperature. The results are reported as mean±SD. Each mean represents the average value of 30 measurements from each independent sample.
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9

Estimating PVA Binder Molecular Weight

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The molecular weight of the PVA binder present on the glass fibre matrix (S14) was estimated by DLS. PVA was extracted and freeze-dried as described above. Solutions of this extracted sample and standards of known polymer size were prepared in water to the concentration of approximately 1.3 mg/mL and passed through 0.22 µm and 300 kDa molecular weight cut-off filters. The sample was then concentrated approximately five-fold from 4 mL to 0.75 mL using a 3 kDa MWCO filter (Vivaspin, GE). Zetasizer Nano ZS and DTS software (Malvern Instruments) was used for measurement of hydrodynamic diameter based on size distribution by volume. Independent duplicate preparations of all standards and samples were tested. Prism 7.0 (GraphPad Software LLC) was used to generate a standard curve plotted between measured hydrodynamic diameter and known average molecular weight (kDa) to interpolate size of the PVA in the extract.
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10

Comprehensive Characterization of AmB Nano-Assemblies

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UV-Visible and fluorescence spectroscopic analysis were employed to ascertain the aggregation state of nano-assemblies. Zeta Potential (ζ-potential) of the nano-particles was determined using DTS software (Malvern Instrument Limited, UK) based on M3-PALS technology. TEM analysis was performed to analyze size and shape of the nano-aggregates. The hydrodynamic particle size of the AmB-NA were determined by DynaPro-TC-04 dynamic light scattering equipment (Protein Solutions, CA) equipped with a temperature-controlled microsampler. The structural characterization of both free as well as nano-particulate form of the drug was performed by X-ray diffraction (XRD). FTIR spectroscopic studies of AmB nano-particles were carried out employing a Perkin-Elmer FTIR Spectrum One spectrophotometer. GC-MS analysis of Aloe vera extract was performed by use of SHIMAZDU QP2010, Column Rtx-5 MS.
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