Ps3 solid phase peptide synthesizer

Manufactured by Protein Technologies

Sourced in Azerbaijan

The PS3 solid phase peptide synthesizer is a laboratory equipment designed for the automated synthesis of peptides. It utilizes the solid phase peptide synthesis (SPPS) technique to assemble amino acids into peptide chains. The core function of the PS3 is to perform the necessary chemical reactions and steps involved in the SPPS process in a controlled and automated manner.

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Lab products found in correlation

0.22 μm filter, by Merck Group (3 mentions)

5 protocols using ps3 solid phase peptide synthesizer

Amyloid-β Peptide Synthesis and Preparation

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Aβ40 peptide was synthesized on a PS3 solid phase peptide synthesizer (Protein Technologies Inc., Woburn, MA) using the standard Fmoc strategy. The resulting crude peptide was purified by reversed-phase high-performance liquid chromatography (RP-HPLC) using a C18 column and characterized by matrix-assisted laser desorption ionization (MALDI) mass spectrometry. The peptide was monomerized as described previously before use (Liu et al., 2018 (link)). Lyophilized peptide powder was dissolved in aqueous NaOH solution (2 mM), and the pH was adjusted to ∼11 by using 100 mM NaOH solution. The solution was sonicated for 1 h in an ice−water bath and then filtered through a 0.22 μm filter (Millipore) and kept on ice before use. The concentration of the peptide solution was determined by using the tyrosine UV absorbance at 280 nm (ε = 1280 M⁻¹ cm⁻¹).

Singh Y., Regmi D., Ormaza D., Ayyalasomayajula R., Vela N., Mundim G., Du D., Minond D, & Cudic M. (2022). Mucin-Type O-Glycosylation Proximal to β-Secretase Cleavage Site Affects APP Processing and Aggregation Fate. Frontiers in Chemistry, 10, 859822.

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Preparation and Characterization of Aβ40 Peptide

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Aβ40 peptide was synthesized on a PS3 solid phase peptide synthesizer (Protein Technologies) using standard Fmoc strategy. The resulting crude peptide was purified by reversed phase high-performance liquid chromatography (RP-HPLC) using a C18 reverse phase column and characterized by matrix-assisted laser desorption ionization mass spectrometry (MALDI). The Aβ40 peptide utilized in the kinetic aggregation assay was monomerized as described previously.^{40 (link)} Briefly, lyophilized Aβ40 powder was dissolved in aqueous NaOH solution (2 mM) and the pH was adjusted to 11 by using 100 mM NaOH solution. The solution was sonicated for 1 h in ice-water bath, then filtered through 0.22-μm filter (Millipore) and kept on ice before use. The concentration of Aβ40 was determined by using the tyrosine UV absorbance at 280 nm (ε = 1,280 M⁻¹cm⁻¹).

Elbassal E.A., Liu H., Morris C., Wojcikiewicz E.P, & Du D. (2015). Effects of Charged Cholesterol Derivatives on Aβ40 Amyloid Formation. The journal of physical chemistry. B, 120(1), 59-68.

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Synthesis and Characterization of Docetaxel-Conjugated Copolymers

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Comonomers of HPMA¹⁶, N-methacryloylglycylglycyl-2-thiazolidine-2-thione (MA-GG-TT), and N-methacryloyl-glycylphenylalanylleucylglycine-docetaxel (MA-GFLG-DOC)^{17 (link)} were synthesized as described previously. DOC was provided by AK Scientific (Mountain View, CA). Free radical precipitation copolymerization using azobisisobutyronitrile (AIBN) as the initiator in methanol at 50°C for 24 hours was used to prepare the copolymers. The product was then precipitated and washed with diethyl ether followed by dialysis against deionized water to remove unreacted comonomers and initiator. The copolymers were lyophilized to obtain the final product. Weight average molecular weight (M_w), number average molecular weight (M_n), and polydispersity index (PDI) is calculated by the ratio of M_w/M_n and were estimated by size exclusion chromatography (SEC).
The GRP78 targeting peptide WDLAWMFRLPVG and corresponding scrambled peptide RWLWVADPFLMG were synthesized via Fmoc chemistry using a Protein Technologies (Tuscon, AZ) PS3 solid phase peptide synthesizer, verified by amino acid analysis and electrospray ionization mass spectrometry (ESI/MS).

Frazier N., Payne A., Dillon C., Subrahmanyam N, & Ghandehari H. (2016). Enhanced Efficacy of Combination Heat Shock Targeted Polymer Therapeutics with High Intensity Focused Ultrasound. Nanomedicine : nanotechnology, biology, and medicine, 13(3), 1235-1243.

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Synthesis and Purification of Tau Peptides

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The tau fragment and mutation pS305 (addition of phosphate group at the side chain of Ser₃₀₅) peptides were synthesized on a PS3 solid phase peptide synthesizer (Protein Technologies Inc., Woburn, MA) using Fmoc chemistry. After cleaving the peptide from the resin using trifluoroacetic acid (TFA) cocktail, the crude peptide was purified by high-performance liquid chromatography (HPLC) using a C₁₈ reverse phase column, where mobile phase A (0.1 % TFA, V/V in water) and B (0.1 % TFA, V/V in acetonitrile) set in gradient program. The mutant was purified by using mobile phase A (0.1 % acetic acid, V/V in water) and B (0.1 % acetic acid, V/V in acetonitrile) set in gradient program. The molecular weight of the peptides was verified by matrix-assisted laser desorption ionization (MALDI) mass spectrometry. After purification, the peptides were lyophilized to obtain dry white samples. For further studies, the peptide aliquots were dissolved in MQ water, and the concentration of the peptide solutions were determined by using the Tyr UV absorbance at 280 nm (ε=1,280 M⁻¹cm⁻¹).

Wilcox A.S., Warrington J.A., Gardiner K., Berger R., Whiting P., Altherr M.R., Wasmuth J.J., Patterson D, & Sikela J.M. (1992). Human chromosomal localization of genes encoding the gamma 1 and gamma 2 subunits of the gamma-aminobutyric acid receptor indicates that members of this gene family are often clustered in the genome.. Proceedings of the National Academy of Sciences of the United States of America, 89(13), 5857-5861.

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Synthetic Aβ Peptide Preparation and Characterization

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The Aβ40 and Aβ40-K16Nle peptides were synthesized on a PS3 solid phase peptide synthesizer (Protein Technologies Inc., Woburn, MA) using the standard Fmoc strategy. The resulting crude peptides were purified by reversed phase high performance liquid chromatography (RP-HPLC) using a C18 column and then characterized by matrix-assisted laser desorption ionization (MALDI) mass spectrometry. The peptides were monomerized as described previously before being used.^{35 (link)} Briefly, lyophilized peptide powder was dissolved in aqueous NaOH solution (2 mM) and the pH was adjusted to ~11 by using 100 mM NaOH solution. The solution was sonicated for 1 h in an ice-water bath, then filtered through a 0.22-μm filter (Millipore) and kept on ice before use. The concentration of the peptide solution was determined by using the tyrosine UV absorbance at 280 nm (ε = 1,280 M⁻¹cm⁻¹).

Elbassal E.A., Morris C., Kent T.W., Lantz R., Ojha B., Wojcikiewicz E.P, & Du D. (2017). Gold Nanoparticles as a Probe for Amyloid-β Oligomer and Amyloid Formation. The journal of physical chemistry. C, Nanomaterials and interfaces, 121(36), 20007-20015.

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