Multipin peptide synthesis at the micromole scale using 2‐hydroxyethyl methacryiate grafted polyethylene supports
- 1 July 1993
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 42 (1) , 1-9
- https://doi.org/10.1111/j.1399-3011.1993.tb00341.x
Abstract
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.Keywords
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