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Prelude peptide synthesizer

Manufactured by Protein Technologies
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Sourced in United States, Azerbaijan

The Prelude peptide synthesizer is a laboratory instrument designed for the automated synthesis of peptides. It performs the chemical reactions necessary to assemble amino acids into desired peptide sequences. The core function of the Prelude is to facilitate the stepwise construction of peptides in a controlled and efficient manner.

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Lab products found in correlation

Fmoc prohypgly oh14, by Bachem (2 mentions) Fmoc glyprohyp oh tripeptide, by Bachem (2 mentions) Ps3 peptide synthesizer, by Protein Technologies (2 mentions) N ε biotin lysine wang resin, by Iris Biotech (2 mentions) Lc 20, by Shimadzu (1 mentions) Modified porcine trypsin, by Promega (1 mentions) 96 well full skirt pcr plates, by Corning (1 mentions) Mycobacterium tuberculosis h37ra, by BD (1 mentions) Incomplete freund s adjuvant, by BD (1 mentions) Pertussis toxin, by List Biological Laboratories (1 mentions) Q tof premier mass spectrometer, by Waters Corporation (1 mentions) Fmoc amino acids, by Protein Technologies (1 mentions) Tamoxifen, by Merck Group (1 mentions) Micromass zq mass spectrometer, by Waters Corporation (1 mentions) Orbitrap elite, by Thermo Fisher Scientific (1 mentions) Tentagel s ram resin, by Rapp Polymere (1 mentions)

17 protocols using prelude peptide synthesizer

1

Solid-phase Peptide Synthesis and Purification

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Solid-phase peptide synthesis was performed at the University of Wisconsin–Madison Biotechnology Center with a Prelude peptide synthesizer from Protein Technologies (Tucson, AZ). Synthetic peptide was purified by HPLC with an LC-20 instrument from Shimadzu. Molecular mass was determined by matrix-assisted laser desorption/ionization–time-of-flight (MALDI–TOF) mass spectrometry on an α-cyano-4-hydroxycinnamic acid matrix with a Voyager DE-Pro instrument at the Biophysics Instrumentation Facility at the University of Wisconsin–Madison.
Ellison A.J., VanVeller B, & Raines R.T. (2015). Convenient Synthesis of Collagen-Related Tripeptides for Segment Condensation. Biopolymers, 104(6), 674-681.
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2

Analytical-grade Chemicals and Isotope-labeled Peptides

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All chemicals used were of analytical grade or better and all solvents were of HPLC-grade or better; all, with the exceptions specified below, were obtained from ThermoFisher-Scientific (St. Waltham, MA, USA): porcine modified trypsin (Promega, Nepean, Ontario, Canada); 96-well full skirt PCR plates (Axygen, Union City, CA, USA); stable isotope-labelled standard peptides were synthesized using Fmoc chemistry on a Prelude peptide synthesizer (Protein Technologies, Inc., Tuscon, AZ).
Guarna M.M., Hoover S.E., Huxter E., Higo H., Moon K.M., Domanski D., Bixby M.E., Melathopoulos A.P., Ibrahim A., Peirson M., Desai S., Micholson D., White R., Borchers C.H., Currie R.W., Pernal S.F, & Foster L.J. (2017). Peptide biomarkers used for the selective breeding of a complex polygenic trait in honey bees. Scientific Reports, 7, 8381.
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3

Peptide Synthesis Protocol using PEG-based Resins

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All CMPs were synthesized on polyethylene glycol-based resins on a Prelude peptide synthesizer from Protein Technologies (Tucson, AZ) using standard Fmoc-based methods at the Peptide Synthesis Facility of the University of Wisconsin–Madison (UW) Biotechnology Center (www.biotech.wisc.edu/services/peptidesynth). Condensation of Fmoc-ProHypGly-OH14 (link) or Fmoc-GlyProHyp-OH tripeptide segments from Bachem (Bubendorf, Switzerland) was employed wherever applicable. Fmoc removal was achieved in piperidine (20% v/v in DMF), and peptide building blocks (4 equiv), activated through treatment with HATU and NMM, were coupled to the free amine of the growing chain for 60 min. Addition onto Pro or Hyp residues were performed through 30-min double couplings. Peptides were cleaved from the resin and deprotected in 95:2.5:2.5 TFA/triisopropylsilane/water (1.5–2.0 mL), precipitated from methyl t-butyl ether below 0 °C, and isolated by centrifugation. The purification and characterization of the resulting peptides is described in the Supplementary Text.
Tanrikulu I.C., Forticaux A., Jin S, & Raines R.T. (2016). Peptide tessellation yields micron-scale collagen triple helices. Nature chemistry, 8(11), 1008-1014.
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4

Peptide Synthesis via Fmoc Chemistry

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The synthesis of all peptide analogs was accomplished using standard Fmoc chemistry. The linear sequences were synthesized on H-Rink Amide ChemMatrix resin using a Protein Technologies Prelude peptide synthesizer. Initially, the resin was swelled in DMF 3 times followed by 5 min washes. Amino acid coupling reactions were accomplished with Fmoc protected amino acids (3 eq), HATU (4 eq), and DIPEA (8 eq), the reagents were dissolved in DMF (5 mL) and the reaction was mixed via nitrogen bubbling for 2 hours at room temperature. Following coupling, the reaction vessel was drained and the resin is washed 3x with DMF, 3x with DCM, and 3x with DMF again. For Fmoc deprotection, the resin is treated with a solution of piperidine (20% in DMF) 2× 10 minutes. Again, the resin is washed as previously stated and the process is repeated for each respective residue in the defined sequence. The sequences of the TAT-labeled peptides (Figures 2 and 3) are as follows: TAT-Pep1, GRKKRRQRRR (PEG2) GVLRKTRHVNILLFMGYST; TAT-PEP17, GRKKRRQRRR (PEG2) VLRKTRHVNILLFMG, TAT-6ALANC3, GRKKRRQRRR (PEG2) GVLAATAAVNALLFAGYST, FAM-TAT-PEP17 and FAM-TAT-PEP6ALANC3 are labelled at the N-terminus with 5-FAM as a fluorescent tag.
Beneker C.M., Rovoli M., Kontopidis G., Röring M., Galda S., Brown S., Brummer T, & McInnes C. (2019). Design and Synthesis of Type IV Inhibitors of BRAF Kinase that block dimerization and overcome paradoxical MEK/ERK activation. Journal of medicinal chemistry, 62(8), 3886-3897.
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5

Multiepitope Peptide Immunization Protocol

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MOG35–55 (MEVGWYRSPFSRVVHLYRNGK), 85b280–294 (FQDAYNAAGGHNAVF) GP61–81 (GLKGPDIYKGVYQFKSVEFD), Aasf24–32 (VSSPAVQES), NP311–325 (QVYSLIRPNENPAHK) and FliC427–441 (VQNRFNSAITNLGNT) peptides were synthesized on a Prelude peptide synthesizer (Protein Technologies, Inc., Tuscon, AZ, USA). For all peptide immunizations, 200 μg of the peptide was emulsified in 375 μg of CFA and injected subcutaneously into the flank of a mouse on days 0 and 7 (150 μl total volume per injection). CFA was made in-house by mixing 20 ml of Incomplete Freund's Adjuvant (Becton Dickinson, Franklin Lakes, NJ, USA) and 100 mg of desiccated Mycobacterium tuberculosis H37 Ra (Becton Dickinson). On days 0 and 2, 300 ng of pertussis toxin (Ptx, List Biological Labratories, Campbell CA, USA) was injected intraperionteallly in all immunizations to compare both the self and foreign immune responses.
Martinez R.J., Andargachew R., Martinez H.A, & Evavold B.D. (2016). Low-affinity CD4+ T cells are major responders in the primary immune response. Nature Communications, 7, 13848.
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6

Peptide Synthesis and Purification Protocol

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Peptides NSFRY-NH2, NSFRA-NH2, NSFRF-NH2, NSAAY-NH2, NSAAA-NH2 and AAAAA-NH2 were synthesized automatically on the Prelude Peptide Synthesizer (Protein Technologies, Inc.) according to the Fmoc strategy [14 ]. Purification of the final products was accomplished by HPLC and pure lyophilized peptides were analyzed by ESI-Q-TOF Premier mass spectrometer to confirm their correct molecular masses.
Wiloch M.Z., Wawrzyniak U.E., Ufnalska I., Piotrowski G., Bonna A, & Wróblewski W. (2016). Redox Activity of Copper(II) Complexes with NSFRY Pentapeptide and Its Analogues. PLoS ONE, 11(8), e0160256.
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7

Induction of Experimental Autoimmune Encephalomyelitis

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EAE was induced with a single (d0) s.c. injection in the hind flank of 300 μg MOG35-55 (MEVGWYRSPFSRVVHLYRNGK) emulsified in CFA containing 5 mg/ml heat-inactivated Mycobacterium tuberculosis (Difco). MOG35-55 peptide and truncated peptides within MOG35-55 (Figure 2A and B) were synthesized on a Prelude Peptide Synthesizer (Protein Technologies, Inc.). Mice also received 250 -300 ng of pertussis toxin (List Biological Laboratories) i.p. on days 0 and 2. Disease severity was assessed using the following scoring rubric: 0, no disease; 0.5 weak tail; 1, flaccid tail, 2, hind limb weakness/poor grip; 3, hind limb paralysis; 4, hind limb paralysis and forelimb weakness; 5, moribund/death.
Kersh A.E., Edwards L.J, & Evavold B.D. (2014). Progression of relapsing-remitting demyelinating disease does not require increased TCR affinity or epitope spread. Journal of immunology (Baltimore, Md. : 1950), 193(9), 4429-4438.
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8

Synthesis and Characterization of Aβ5–9 Peptide

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The Aβ5–9 peptide
(Arg–His–Asp–Ser–Gly–NH2) was synthesized on a Prelude peptide synthesizer (Protein
Technologies, Inc. Tucson, AZ) according to the Fmoc strategy.21 The peptide crude was purified by HPLC on a
Breeze system (Waters) equipped with a Vydac semipreparative column
(5 mm particle size, 10 × 250 mm). The mobile phase was a linear
gradient of solution B [0.1% (v/v) TFA/90% (v/v) acetonitrile/9.9%
(v/v) water] in solution A [0.1% (v/v) TFA/99.9% (v/v) water]. The
purity of the lyophilized peptide was verified by a Q-Tof Premier
mass spectrometer (Waters) exhibiting correct molecular masses.
Tobolska A., Wezynfeld N.E., Wawrzyniak U.E., Bal W, & Wróblewski W. (2021). Tuning Receptor Properties of Metal–Amyloid Beta Complexes. Studies on the Interaction between Ni(II)–Aβ5–9 and Phosphates/Nucleotides. Inorganic Chemistry, 60(24), 19448-19456.
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9

Solid-Phase Synthesis of msPapA

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msPapA was prepared by solid phase peptide synthesis using either a Prelude peptide synthesizer (Protein Technologies Inc) or a Chorus peptide synthesizer (Protein Technologies Inc). The syntheses and subsequent purification followed the same procedure as reported (40 (link)). All of the Fmoc-amino acids were purchased from Protein Technologies Inc. The msPapA was quantified by dry weight and the Y17W msPapA was quantified by its absorbance at 280 nm.
Eastman K.A., Jochimsen A.S, & Bandarian V. (2023). Intermolecular electron transfer in radical SAM enzymes as a new paradigm for reductive activation. The Journal of Biological Chemistry, 299(9), 105058.
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10

Peptide Synthesis for T Cell Priming and EAE

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Peptides used for T cell priming and EAE induction were generated in our laboratory with the Prelude peptide synthesizer (Protein Technologies, Inc) with the following sequences; MOG35-55 (MEVGWYRSPFSRVVHLYRNGK), NFM15-35 (RRVTETRSSFSRVSGSPSSGF), NFM15-35 T20Y (RRVTEYRSSFSRVSGSPSSGF), NFM15-35 E19W, T20Y (RRVTWYRSSFSRVSGSPSSGF), NFM15-35 S23P (RRVTETRSPFSRVSGSPSSGF), NFM15-35 S28V (RRVTETRSSFSRVVGSPSSGF).
Blanchfield L., Sabatino JJ J.r., Lawrence L, & Evavold B.D. (2017). NFM cross-reactivity to MOG does not expand a critical threshold level of high affinity T cells necessary for onset of demyelinating disease. Journal of immunology (Baltimore, Md. : 1950), 199(8), 2680-2691.
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