Solid-phase peptide synthesis using a new PS-TTEGDA resin: Synthesis of pardaxin (1-26)

Tetraethyleneglycol diacrylate (4%)-crosslinked polystyrene has been used a s solid support for peptide synthesis. This resin undergoes extensive swell ing in a broad range of solvents with varying polarity. The resin beads aft er chloromethylation have been used in the synthesis of 26-residue peptide corresponding to the hydrophobic amino terminal region of pardaxin from Par dachirus pavoninus (H-Gly-Phe-Phe-Ala-Leu-Ile-Pro-Lys-Ile-lle-Ser-Ser-Pro-L eu-Phe-Lys-Thr-Leu-Leu-Ser-Ala-Val-Gly-Ser-Ala-Leu-OH). The first amino aci d Boc-Leu is attached to the chloromethyl resin by cesium salt method in a capacity of 1.8 mmol/g and the remaining amino acids are incorporated into this support following the standard solid-phase methodology of peptide synt hesis. The completely deprotected peptide is cleaved from the resin by trif luoroacetic acid, isolated in solid form, purified by FPLC and characterise d by amino acid analysis and gas phase protein sequencing. The free peptide has an alpha-helical conformation as revealed by CD measurement. This synt hesis illustrates the application of the novel flexible support for the syn thesis of 26-residue bio-active peptide.