Measurements were performed on a Zetasizer Nano-S system (Malvern Instruments, Worcestershire, UK) equipped with a 4 mW He-Ne laser. Samples containing the mixture of peptides and vesicles were placed in a low volume quartz cell equilibrated at 25 °C, and the light scattered backward was collected at an angle of θ = 173°. Data analysis was performed with the DTS Malvern software implemented on a personal computer.
Zetasizer nano s system
Manufactured by Malvern Panalytical
Sourced in United Kingdom
The Zetasizer Nano-S system is a laser diffraction-based instrument designed to measure the size and size distribution of particles, molecules, and materials in suspension or solution. The system uses the technique of dynamic light scattering to determine the hydrodynamic size of the sample. It is capable of measuring particle sizes ranging from 0.3 nanometers to 10 micrometers.
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Lab products found in correlation
Zetasizer software version 7, by Malvern Panalytical (3 mentions)
Zetasizer software, by Malvern Panalytical (1 mentions)
Superdex s200 16 60, by GE Healthcare (1 mentions)
Akta pure system, by GE Healthcare (1 mentions)
D saccharose, by Carl Roth (1 mentions)
Jsm 7610, by JEOL (1 mentions)
0.1 μm filter, by Merck Group (1 mentions)
Dts1070, by Malvern Panalytical (1 mentions)
Uranyl acetate, by Merck Group (1 mentions)
Alliance ld2, by Uvitec (1 mentions)
N hydroxysuccinimide, by Merck Group (1 mentions)
Jem 2010f, by JEOL (1 mentions)
Uv 1800 spectrometer, by Shimadzu (1 mentions)
F 4500 fluorescence spectrometer, by Hitachi (1 mentions)
Low volume quartz cuvette, by Hellma (1 mentions)
19 protocols using zetasizer nano s system
1
Dynamic Light Scattering of Peptide-Vesicle Mixtures
2
Protein Oligomer Size Assessment by DLS
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Prior to the experiments, stock protein solutions were centrifuged at 10,000 rpm and 4 °C for 10 min to remove precipitates and equilibrated to the measurement temperature for 10 min. Oligomer size was assessed using dynamic light scattering (DLS) with a Malvern Zetasizer Nano-S system (Malvernpanalytical; Malvern, UK) at a protein concentration of 50 μM in Tris-sucrose buffer at 25 and 37 °C, respectively. Protein samples (100 μL) were measured at least three times using disposable plastic cuvettes and the hydrodynamic radius (Rh) was calculated from size–number plots using the Stokes–Einstein equation.
3
Polyplex Size and Polydispersity Measurement
4
Nanoparticle Characterization by DLS
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Particle-size distribution and zeta potential were determined by dynamic light scattering (DLS) by using a Zetasizer Nano-S system (Malvern Instruments, UK). The self-optimization routine in the Zetasizer software (Version 3.30, Malvern Panalytical Ltd., Malvern, UK) was used for all measurements, and the zeta-potential was calculated according to the solutions theory. After a 100-fold dilution with a low ionic strength (2 mM) phosphate buffer at pH 7, measurements were performed at 25 °C in triplicate.
5
Nanoparticle Characterization by DLS
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Hydrodynamic diameter, polydispersity index (PDI), and z-potential were determined by dynamic light scattering (DLS). Measurements were performed with a Zetasizer Nano-S system (Malvern Instruments, Malvern, UK). The self-optimization routine in the Zetasizer software (v 7.13.0.9398) was used for all measurements, and the z-potential was calculated according to the Smoluchowsky theory. Samples were diluted with a low ionic strength phosphate buffer (1.13 mM KH2PO4, pH = 7) and measured at 25 °C in triplicate. Results appeared as the mean value ± standard deviation (SD). During the colloidal stability studies, the pH effect was analyzed using buffers with identical ionic strength (0.002 M), while the ionic strength effect was analyzed at stable neutral pH of 7. The colloidal stability of the prepared systems in PBS (pH = 7.4 and 150 mM) was also determined.
6
PF4 Antibody Complex Formation
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PF4 and antibodies were centrifuged at 4 °C for 20 min at 14.8 × 103 g min−1 to remove aggregates if any. To form complexes of PF4 with antibodies, PF4 (5 μg ml−1 final) was incubated with affinity purified antibodies (10 μg ml−1 final) at RT for 30 min before measurements (Supplementary Fig. 6c ). To investigate whether control IgG, group-1, group-2, or group-3 ABS bind to PF4/group-3 ABS complexes, preformed PF4/group-3 ABS complexes were incubated with these antibodies (10 μg ml−1 final) for 30 min at RT before measurements. DLS-fixed scattering angle Zetasizer Nano-S system (Malvern Instruments Ltd., Malvern, UK) and disposal cuvettes were used. The Z-average size of PF4, antibodies or their complexes in terms of the hydrodynamic diameter were measured in PBS at 25 °C and light scattering was detected at 173° using 10 repeating measurements. Data analysis was performed using the Zetasizer software, Version 7.11 (Malvern Instruments Ltd., Malvern, UK).
7
Characterization of Δ133p53β by SEC and DLS
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Characterization of Δ133p53β was done by SEC and DLS. SEC was performed on a Superdex S200 16/60 (HiLoad 16/600 Superdex 200 pg, GE Lifescience) on an AKTA Pure system (GE Lifescience). The protein was concentrated and injected on the column with a 5 ml loop equilibrated with buffer A. DLS was performed using the Zetasizer NaNo-S system (Malvern Instruments) on the SEC maximum peak. Data were collected in 3 consecutive runs of 15 repeated measurements at 20 °C. The sample volume used was 150 µl at 0.8 mg/ml.
8
DLS Analysis of ChAdOx1 nCoV-19 Interactions
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All dynamic light scattering (DLS) measurements were performed in a fixed scattering angle Zetasizer Nano-S system (Malvern Instruments Ltd, Malvern, United Kingdom). The hydrodynamic diameter (nm) was measured at 25°C, and light scattering was detected at 173° using 3 repeating measurements consisting of 12 runs. Experimental data were collected from 4 independent experimental replicates. For all DLS measurements, ChAdOx1 nCoV-19 was diluted at a ratio of 1:10 in sterile-filtered 0.9% NaCl supplemented with 4 mg/mL D (+) saccharose (ribonuclease/DNase free; catalog no. 9097.1; Carl Roth GmbH, Germany). Assessment of changes in the hydrodynamic diameter of ChAdOx1 nCoV-19 vector in the presence of PF4 was performed by incubating 10 µg/mL of human PF4 (Chromatec, Greifswald, Germany) with ChAdOx1 nCoV-19 vector at room temperature (RT) for 2 minutes before DLS measurements. Anti-PF4 mouse monoclonal IgG (Clone RTO, catalog no. MA5-17639, Invitrogen) affinity-purified anti-PF4 IgG antibodies from VITT sera, and control human IgG from a healthy individual were purified by Protein G affinity purification and were used at 5 µg/mL final concentration. Double-stranded annealed DNA 25-mer was used at 0.5 µg/mL. Dissociation of complexes formed between ChAdOx1 nCoV-19 vector and added components was achieved by 100 IU/mL unfractionated heparin (UFH; Ratiopharm GmbH, Ulm, Germany).
9
Characterization of Nanoparticle Properties
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NPs’ PSD (and PDI) was determined by dynamic light scattering (DLS) using a Zetasizer Nano-S system by Malvern Instruments (Malvern, UK). For the preparation of samples, a 100-fold dilution with low ionic strength (2 mM) phosphate buffer at pH 7 was performed. All measurements were conducted at 25 °C in triplicate.
NP’s morphology was evaluated via scanning electron microscopy (SEM). Briefly, SEM images were acquired with an ultra-high resolution Schottky Field Emission Scanning Electron Microscope, model JSM-7610, by JEOL (Akishima, Tokyo, Japan). For the measurements, a drop of each NPs (suspended in water) was placed in the holder and left to evaporate. All samples were covered with carbon to establish good conductivity. During the measurements, the SEMs operating conditions were: 20 kV accelerating voltage, 45 nA probe current, and 60 s counting time.
NP’s morphology was evaluated via scanning electron microscopy (SEM). Briefly, SEM images were acquired with an ultra-high resolution Schottky Field Emission Scanning Electron Microscope, model JSM-7610, by JEOL (Akishima, Tokyo, Japan). For the measurements, a drop of each NPs (suspended in water) was placed in the holder and left to evaporate. All samples were covered with carbon to establish good conductivity. During the measurements, the SEMs operating conditions were: 20 kV accelerating voltage, 45 nA probe current, and 60 s counting time.
10
Liposome Size Characterization
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Liposomes were analyzed on a Zetasizer Nano S system (Malvern Instruments). Single measurements consisted of 20 repetitions over 10 min. Error was calculated as the standard error of averaged values from at least three independent measurements.
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