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 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.
Valerio
R M
RM
Chiron Mimotopes Pty Ltd., Clayton, Victoria, Australia.
Bray
A M
AM
Campbell
R A
RA
Dipasquale
A
A
Margellis
C
C
Rodda
S J
SJ
Geysen
H M
HM
Maeji
N J
NJ
D000595:Amino Acid Sequence; D005069:Evaluation Studies as Topic; D008689:Methacrylates; D008722:Methods; D008832:Microchemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011095:Polyethylenes
D008689:Methacrylates; D009842:Oligopeptides; D010455:Peptides; D011095:Polyethylenes; C005044:hydroxyethyl methacrylate