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Fmoc protected α amino acids

Manufactured by Chem-Impex

Fmoc protected α-amino acids are commonly used as building blocks in solid-phase peptide synthesis. They provide a temporary protecting group for the amino group of amino acids, allowing for the selective coupling of amino acids during the peptide synthesis process.

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6 protocols using fmoc protected α amino acids

1

Fmoc-protected α-amino acid peptide synthesis

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Fmoc–protected α-amino acids and Rink amide resin used for γ-AApeptide synthesis were purchased from Chem-Impex International, Inc. All chemicals and solvents used were purchased from Aldrich or Fisher and were used without further purification.
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2

Solid-Phase Synthesis of Sulfono-γ-AApeptides

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All reagents and solvents were purchased from Fisher or Aldrich and used without further purification. Fmoc protected α-amino acids and Rink-amide resin (0.6 mmol/g, 200‒400 mesh) were purchased from Chem-Impex International, Inc. The sulfono-γ-AApeptide building block synthesized on solid support Rink-amide resin as previously reported31 (link),32 (link). Full details of the chemical synthesis and purification are given in the Supplementary Methods.
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3

Solid-Phase Peptide Synthesis and Purification

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All reagents and solvents were purchased from Fisher or Aldrich and used without further purification. Fmoc protected α-amino acids and Rink-amide resin (0.6 mmol/g, 200-400 mesh)
were purchased from Chem-Impex International, Inc. Solid-phase syntheses of the compounds were carried out in the peptide synthesis vessel on a Burrell Wrist-Action shaker. The products were analyzed and purified on a Waters Breeze 2 HPLC system installed with both analytic module
(1 mL/min) and preparative module (16 mL/min), by employing a method using 5-100% linear gradient of solvent B (0.1% TFA in acetonitrile) in solvent A (0.1% TFA in water) over 40 min, followed by 100% solvent B over 10 min. The desired fractions were collected and lyophilized on a Labconco lyophilizer. High-resolution MS was conducted on an Agilent 6540 LC/QTOF system.
1 HNMR spectra were acquired with the WET solvent suppression at Varian 600 MHz.
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4

Solid-Phase Peptide Synthesis Protocol

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Rink-amide resin (0.64 mmol g−1, 200–400 mesh) and Fmoc protected α-amino acids were purchased from Chem-impex Int’l Inc. Solvents, coupling reagents, and other chemicals of reagent grade were purchased from either Fisher Scientific or Sigma-Aldrich. Column chromatography was carried out with silica gel (200–300 mesh). All compounds were synthesized by using solid-phase peptide synthesis. The compound was synthesized in a peptide reaction vessel clamped on a Burrell wrist-action shaker and purified on a High-Performance Liquid Chromatography (HPLC) system with both analytical and preparative functions. The final product’s molecular weight was confirmed by using a Bruker AutoFlex MALDI-TOF mass spectrometer, and the desired final pure products were dried on a Labcono lyophilizer.
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5

Synthesis and Purification of Heterogeneous Peptides

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All Fmoc-protected α-amino acids and Rink-amide resin (0.7 mmol/g, 200–400 mesh) were purchased from Chem-Impex International, Inc. Other solvents and reagents were purchased from either Sigma-Aldrich or Fisher Scientific and used without further purification. Solid-phase synthesis of 1:1 α/sulfono-γ-AA peptides were carried out in the peptide synthesis vessel on a Burrell Wrist-Action shaker. The sequences were purified on a Waters Breeze 2 HPLC system, and desired fractions were collected and lyophilized on a Labcono lyophilizer. The molecular weight of the heterogeneous peptides was obtained on an Applied Biosystems 4700 Proteomics Analyzer.
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6

Solid-Phase Peptide Synthesis Protocol

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All Fmoc protected α-amino acids and Rink-amide resin (0.7 mmol/g, 200–400 mesh) were purchased from Chem-Impex International, Inc. Solvents and other reagents were purchased from either Sigma-Aldrich or Fisher Scientific and were used without further purification. Solid-phase synthesis of the compounds was carried out in the peptide synthesis vessel on a Burrell wrist-action shaker. The products were purified on a Waters Breeze 2 HPLC system, and lyophilized on a Labconco lyophilizer. The purity of the compounds was determined to be >95% by analytical HPLC (1 mL/min flow, 5–100% linear gradient of solvent B (0.1% TFA in acetonitrile) in A (0.1% TFA in water) over 40 min was used). The NMR spectra were obtained on a Varian Inova 400 instrument.
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