Peptides were synthesized on a PS3 automated peptide synthesizer (Protein Technologies, MA) using standard 9-fluorenylmethoxy-carbonyl (Fmoc) solid phase synthesis protocols and Fmoc-protected amino acids from either Bachem Americas (Torrence, CA) or AnaSpec (Fremont, CA). Before use, all peptide samples were further purified by reverse-phase high-performance liquid chromatography and verified by mass spectrometry. All peptide samples used in the pH titration measurements were prepared by dissolving lyophilized peptides into either acidic (25 mM H3PO4) or basic (25 mM NaOH) Millipore water, and the final concentration of each sample (20 μM) was determined optically using the absorbance of PheCN at 280 nm and a molar extinction coefficient of 850 M−1 cm−1 [7 (link)].
Ps3 automated peptide synthesizer
Manufactured by Protein Technologies
Sourced in United States
The PS3 automated peptide synthesizer is a laboratory instrument designed for the automated synthesis of peptides. It performs the sequential coupling of amino acids to assemble peptide chains using a solid-phase synthesis approach. The PS3 automates the repetitive steps involved in peptide synthesis, providing a programmable and consistent method for producing peptide samples.
Automatically generated - may contain errors
Lab products found in correlation
Fmoc protected amino acids, by Protein Technologies (1 mentions)
High performance liquid chromatography (hplc), by Waters Corporation (1 mentions)
Liberty blue microwave peptide synthesizer, by CEM Corporation (1 mentions)
Rink amide mbha resin, by Merck Group (1 mentions)
N succinimidyl methacrylate, by Tokyo Chemical Industry (1 mentions)
Agilent 1260 hplc, by Agilent Technologies (1 mentions)
10 protocols using ps3 automated peptide synthesizer
1
Peptide Synthesis and Purification
2
Solid-Phase Synthesis of JZTX-V
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The solid-phase synthesis of JZTX-V was carried out by referring to the methods of Zeng et al. [23 ], of which steps are briefly described as follows. First, according to the primary sequence of JZTX-V, the Fmoc-protected amino acids were used to synthesize the liner JZTX-V on the PS3™ automated peptide synthesizer (Protein Technologies, USA). Second, the synthetic linear peptide was oxidatively refolded. Finally, the end product was purified by HPLC (Waters, USA) to 99% purity.
3
Synthesis and Purification of Aβ40 Peptides
4
Synthesis and Purification of Z34C Peptides
5
PNA-loaded Porous Silica Nanoparticles
6
Automated Peptide Synthesis and Purification
7
Solid-Phase Synthesis of Peptide Analogs
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All peptide analogs of APP were synthesized using standard Fmoc chemistry and solid-phase peptide synthesis (SPPS) on a PS3 automated peptide synthesizer (Protein Technologies Inc., Tucson, AZ). The amino acid couplings on the synthesizer were done using a 4-fold excess of amino acids, HOBt, and HCTU, in the presence of 0.4 MN-methylmorpholine (NMM) in DMF. The Fmoc protecting group was removed using 20% piperidine in DMF. For glycopeptides, at the desired site of glycosylation, the Fmoc-protected pentafluorophenyl ester of Ser-O-GalNAc 1 ) and/or Thr-O-GalNAc 2 ) was coupled manually using a 1.5-fold excess, in the presence of DIPEA (pH 8) for 16 h. After coupling was confirmed using the ninhydrin test, the remainder of the peptide’s amino acid sequence was completed on the PS3. All the (glyco)peptides were cleaved from the resin using a TFA/thioanisole/water mixture in 95:2.5:2.5 ratio for 3 h, followed by precipitation in cold methyl-tert-butyl-ether (MTBE) to precipitate the crude (glyco)peptide. For glycopeptides, the acetylated crude was deprotected using 0.01 M NaOH solution for 15 min to remove all the O-acetyl groups on the glycan moiety attached to the peptide sequence. Lastly, the crude was lyophilized to yield the final crude deacetylated glycopeptide or its nonglycosylated counterpart.
8
Synthesis of Cyclic Peptide OL1 and Analogues
9
Automated Synthesis of Bioactive Peptide Monomers
10
Characterization and Synthesis of LTB Peptide
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Once we obtained the open reading frame of LTB, we picked the putative mature peptide sequence of LTB (GLFSVVKGVLKGVGKNVSGSLLDQLKCKISGGC) for BLAST comparison (https://blast.ncbi.nlm.nih.gov/Blast.cgi , BLASTP 2.9.0+, Database nr_v5). The structural similarity of LFB was used for classification into existing peptide families or a structurally-novel peptide family. We also synthesized LFB using an automated PS3 peptide synthesizer (Protein Technologies, Woburn, MA, USA). After synthesis, synthesized replicates of LFB were further purified by RP-HPLC and confirmed its authenticity by MALDI-TOF MS. A sample of this fraction was subjected to MALDI-TOF mass spectrometry using a Perseptive Biosystems Voyager DE mass spectrometer (Applied Biosystems, Warrington, UK) in positive detection mode using α-cyanohydroxycinnamic acid as matrix.
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