Polysorbate 20
It is a polyethoxylated sorbitan ester derived from polyethylene glycol and oleic acid.
Polysorbate 20 is known for its ability to solubilize and stabilize various compounds, making it a valuable ingredient in a range of products, from topical creams to drug formulations.
Its versatility and effectiveness have made it a common component in many formulations, contributing to its widespread use and importance in scientific research and development.
Most cited protocols related to «Polysorbate 20»
PLGA nanoparticles were prepared by an “oil-in-water” solvent evaporation method, using polysorbate 20 as emulsifying agent. Briefly, 1 ml of dichloromethane containing 50 mg of PLGA and 2 ml 1% (w/v) polysorbate 20 were emulsified using an ultrasonic processor for 15 s at 70 W (Branson Instruments, Connecticut, USA). The emulsion was transferred to 50 ml of 0.02% (w/v) polysorbate 20 in water and stirred at 50°C for 1 hr. The resulting PLGA nanoparticles were collected by centrifugation (8,000 g for 10 min) and washed twice in distilled water to remove excess polysorbate 20. The sample was diluted 2000-fold with deionized water before the measurements.
Cationic liposomes were prepared by the film-hydration-rehydration method and sized by sonication. In detail, a lipid film was formed by solvent evaporation of a chloroform solution of EPC, DOPE and DOTAP in a rotary evaporator at 37°C. To prepare 1 ml of liposome dispersion, a total amount of 28 μmol lipid was used at a EPC/DOPE/DOTAP molar ratio of 4/2/1. The film was hydrated in 1 ml of 20 mM HEPES, 5% glucose, pH 7.4, and the dispersion was equilibrated for 1 hr at room temperature. The dispersion was then sonicated twice for 30 s, with 30 s interval, using a Branson Sonifier 250 (Branson Ultrasonics, Danbury, UK), with 3 mm microtip at 20 mW energy output. The sample was diluted 10,000-fold with deionized water before the measurements.
All the buffers used in this section were filtered using a 0.22-μm PES low binding syringe-driven filter unit (Millex™ GP, Millipore, Ireland), and the absence/very low content of submicron particles was confirmed by their visualization in the NanoSight sample chamber.
Most recents protocols related to «Polysorbate 20»
Example 6
Compound 3 was generated from the purification process of IL-2 mutein Ala-M1 polymer prodrug 5. During separation of compound 5 on a Capto MMC ImpRes resin the later eluting peak which contains 3 was collected. The collected fraction was diluted with 10 mM succinic acid, pH 5.0 to lower the conductivity to approx. 14 mS/cm and further purified on a Äkta system equipped with a HiScreen Capto Blue column using buffer A (20 mM sodium phosphate, pH 7.5), buffer B (20 mM sodium phosphate, 1 M NaCl, pH 7.5) and a gradient from 0 to 50% buffer B in 6 column volumes. The main peak was collected and concentrated using Amicon Ultra centrifugal device (3 kDa MWCO). The concentrated solution was buffer exchanged to 10 mM Hepes, 150 mM NaCl, 3 mM EDTA, 0.05% polysorbate 20, pH 7.4 by using an Äkta system and a HiPrep 26/10 column and the concentration was adjusted to 0.25 mg/mL to give compound 3.
Example 2
Evaluation of 10 mM acetate, 75 mM L-arginine, 2.4% (w/v) sorbitol, 0.01% (w/v) polysorbate 20 excipients formulations and a 10 mM acetate, 5% (w/v) sorbitol, 0.01% (w/v) polysorbate 20 excipients formulation, each with high concentration (120 mg/mL) denosumab, at a temperature of 37° C. for up to 1 month revealed the effects of pH and amino acid aggregation inhibitor on the rate and extent of HMWS formation. The formulations tested are described in Table 2 below. All buffer and excipient values quoted are for the buffer and excipient concentrations that the antibody is diafiltered against.
To prepare test samples M-Q, a 3 mL aliquot of denosumab at 70 mg/mL in acetate, pH 5.2 was dialyzed against 500 mL of DF buffer described below, with a total of 3 buffer changes to achieve a 1 million fold dilution of the previous formulation to ensure complete buffer exchange. The material was then over-concentrated using centrifuge-concentrator, followed by a dilution to 120 mg/mL and the addition of polysorbate 20 to a final concentration of 0.01%.
As the solution pH decreased, there was an increase in formation of large aggregates. At pH below 4.8, and especially 4.5, large aggregates were the dominant HWMS, with a dramatic increase for the test formulation at pH 4.5. As shown in
However, as the pH was increased, there was generally a resulting increase in the dimer species. As shown in
The presence of arginine in formulation O at a concentration of 75 mM resulted in approximately 0.3% and 25% reductions in the amounts of the dimer species and its kinetic rate of formation, respectively, after 1 month at 37° C. when compared to formulation P having the same pH, but without arginine.
Formulations were created by buffer exchanging the starting material (1.0 mL of PF-06439535) using 0.5–3 mL Slide-A-Lyzer cassettes (Thermo Fisher Scientific, Waltham, MA, USA) into the proper buffers/pH. After dialysis, the protein concentration was verified, followed by sterile filtration, and filled into vials to be stored in designated storage conditions.
The excipients used in buffer preparation were analytical grade sourced from various reputable vendors in the United States (US). The formulations were stored at 40 °C for up to 12 weeks to determine the optimal buffer and pH under stressed conditions.
where “DF” is the dilution factor. The release data were fitted to different kinetic models “(Zero–order, First–order, Higuchi–Matrix Square–Root, Hixson–Crowell Cube–Root, and Korsmeyer–Peppas)”. The best–fitted kinetic model for LZ release from CSNPs was categorized based on the highest value of the coefficient of correlation (R2). From the slopes and intercepts of the different release plots, the release exponent (n-value) was calculated [40 (link)]. The n-value would suggest the mechanism of LZ release from CSNPs [13 (link),41 ,42 (link)].
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More about "Polysorbate 20"
It is a polyethoxylated sorbitan ester derived from polyethylene glycol and oleic acid.
Polysorbate 20 is prized for its ability to solubilize and stabilize various compounds, making it a valuable ingredient in a range of products, from topical creams to drug formulations.
Its versatility and effectiveness have made it a common component in many formulations, contributing to its widespread use and importance in scientific research and development.
Polysorbate 20 is often used as a stabilizer for proteins like bovine serum albumin (BSA) and vitronectin, and can also be found in PVDF membranes and Biacore T200 systems.
It is known for its compatibility with a variety of materials, including POLYSORP™ plates, and can be used to improve the solubility and dispersion of compounds in aqueous solutions.
The use of Polysorbate 20 is not without its challenges, however.
Researchers must be mindful of the potential for contamination and potential interactions with other ingredients.
Careful optimization of Polysorbate 20 concentrations and formulations is often required to achieve the desired results.
Overall, Polysorbate 20 is a versatile and important ingredient in many scientific and industrial applications.
Understanding its properties, uses, and limitations is crucial for researchers and formulators working with a wide range of compounds and products.