The peptides were synthesized by manual fluorenylmethyloxycarbonyl (Fmoc) solid phase synthesis at elevated temperature using our previously reported protocol optimized for hydrophobic peptides36 (link). Cleavage of the peptides from resin and side chain deprotection was simultaneously achieved by treatment with a mixture of trifluoroacetic acid (TFA)/H2O/triisopropyl silane (TIS) (95:2.5:2.5, v/v) for 2 hours at room temperature. The crude peptides were precipitated and washed with cold methyl-tert-butyl ether, and purified on a preparative reverse phase HPLC system (Varian ProStar 210) with a C4 preparative column (Vydac), using a linear gradient of solvent A (0.1% TFA in Millipore H2O) and solvent B (90% CH3CN, 10% H2O, 0.1% TFA). The identities and the purities of the purified peptides were confirmed by MALDI-TOF mass spectrometry using a Bruker Autoflex III Smartbeam MALDI-TOF mass spectrometer. Purity of the obtained peptides was additionally evaluated on a Shimadzu Prominence UFLC instrument with an analytical Zorbax Eclipse XDB-C18 column (4.6 mm×150 mm).
Uflc instrument
Manufactured by Agilent Technologies
The UFLC instrument is an analytical tool designed for ultra-fast liquid chromatography. It provides high-speed separation and analysis of complex samples, enabling efficient and rapid processing of experimental data.
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2 protocols using uflc instrument
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Hydrophobic Peptide Synthesis and Purification
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Hydrophobic Peptide Synthesis and Purification
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The peptides were synthesized by manual fluorenylmethyloxycarbonyl (Fmoc) solid phase synthesis at elevated temperature using our previously reported protocol optimized for hydrophobic peptides36 (link). Cleavage of the peptides from resin and side chain deprotection was simultaneously achieved by treatment with a mixture of trifluoroacetic acid (TFA)/H2O/triisopropyl silane (TIS) (95:2.5:2.5, v/v) for 2 hours at room temperature. The crude peptides were precipitated and washed with cold methyl-tert-butyl ether, and purified on a preparative reverse phase HPLC system (Varian ProStar 210) with a C4 preparative column (Vydac), using a linear gradient of solvent A (0.1% TFA in Millipore H2O) and solvent B (90% CH3CN, 10% H2O, 0.1% TFA). The identities and the purities of the purified peptides were confirmed by MALDI-TOF mass spectrometry using a Bruker Autoflex III Smartbeam MALDI-TOF mass spectrometer. Purity of the obtained peptides was additionally evaluated on a Shimadzu Prominence UFLC instrument with an analytical Zorbax Eclipse XDB-C18 column (4.6 mm×150 mm).
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