Multipin peptide synthesis at the micromole scale using 2-hydroxyethyl methacrylate grafted polyethylene supports.

Autor: Valerio RM; Chiron Mimotopes Pty Ltd., Clayton, Victoria, Australia., Bray AM, Campbell RA, Dipasquale A, Margellis C, Rodda SJ, Geysen HM, Maeji NJ
Jazyk: angličtina
Zdroj: International journal of peptide and protein research [Int J Pept Protein Res] 1993 Jul; Vol. 42 (1), pp. 1-9.
DOI: 10.1111/j.1399-3011.1993.tb00341.x
Abstrakt: The multipin peptide synthesis procedure has been adapted to allow the synthesis of peptides at micromole loadings. The original solid pin support was replaced with a detachable crown-shaped polyethylene support with an increased surface area. In addition, the polyethylene crowns were radiation-grafted with 2-hydroxyethyl methacrylate monomer instead of acrylic acid to yield hydroxy functionalized supports with a larger 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 attachment. Peptides varying in length from 10 to 25 residues were assembled at a number of loadings from 1.0 to 2.2 mumol. Purity of peptides at all loadings was equal to, and in some instances superior to, that achieved on conventional solid-phase supports.
Databáze: MEDLINE