MULTIPIN PEPTIDE-SYNTHESIS AT THE MICROMOLE SCALE USING 2-HYDROXYETHYL METHACRYLATE GRAFTED POLYETHYLENE SUPPORTS

The multipin peptide synthesis procedure has been adapted to allow the synthesis of peptides at micromole loadings. The original solid pin s upport was replaced with a detachable crown-shaped polyethylene suppor t with an increased surface area. In addition, the polyethylene crowns were radiation-grafted with 2-hydroxyethyl methacrylate monomer inste ad of acrylic acid to yield hydroxy functionalised supports with a lar ger concentration of polymer and hence a larger peptide capacity. Fmoc -beta-Alanine was directly esterified to the HEMA hydroxy groups with subsequent addition of a diketopiperazine-forming handle for peptide a ttachment. Peptides varying in length from 10 to 25 residues were asse mbled at a number of loadings from 1.0 to 2.2 mumol. Purity of peptide s at all loadings was equal to, and in some instances superior to, tha t achieved on conventional solid-phase supports. (C) Munksgaard 1993.