<span style="font-size:12.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-ansi-language: EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:AR-SA" lang="EN-IN">Solid-phase peptide synthesis using a new PS-TTEGDA resin: Synthesis of pardaxin (1-26)</span>

Abstract

Tetraethylcneglycol diacrylate (4%)-crosslinked polystyrene has been used as solid support for peptide synthesis. This resin undergoes extensive swelling in a broad range of solvents with varying polarity. The resin beads after chloromethylation have been used in the synthesis of 26-residue peptide corresponding to the hydrophobic amino terminal region of pardaxin from <i>Pardachirus pavoninus </i>(H-Gly-Phe-Phe-Ala-Leu-Ile-Pro-Lys- Ile-Ile-Ser-Ser-Pro-Leu-Phe-Lys-Thr-Leu-Leu-Ser-Ala-Val-Gly-Ser-Ala-Leu-OH). The first amino acid Boc-Leu is attached to the chloromethyl

<span style="font-size:12.0pt;font-family:" times="" new="" roman";="" mso-fareast-font-family:"times="" roman";mso-ansi-language:en-in;mso-fareast-language:="" en-in;mso-bidi-language:ar-sa"="" lang="EN-IN">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 synthesis. The completely deprotected peptide is cleaved from the resin by trifluoroacetic acid, isolated in solid form, purified by FPLC and characterised by amino acid analysis and gas phase protein sequencing. The free peptide has an <img src='/image/spc_char/alpha.gif' border=0>-helical conformation as revealed by CD measurement. This synthesis illustrates the application of the novel flexible support for the synthesis of 26-residue bio-active peptide.</span>