Synthesis of peptide gels for the investigation of oligopeptide–oligonucleotide interactions

Peptide gels usable as protein model systems have been synthesized by a cross‐linking copolymerization of acryloyl substituted peptides with 1,4‐tetramethylene dimethacrylate. A specially adapted approach to peptide synthesis allows the removal of the amino terminal Cbo group at the end of the peptide synthesis, followed by the introduction of an acryloyl group. The polymerizable peptide monomers obtained can be transferred into insoluble peptide gels by radical copoylmerization with cross‐linking agents. After cleavage of the protecting groups of the side chains, these peptide gels can be used both as protein model systems for investigating peptide–oligonucleotide interaction and as sorbents for affinity chromatography. The preparation and characterization of the peptide gels Ala‐Lys‐Glu‐Lys‐Ala‐OMe (I), Ala‐Arg‐Glu‐Arg‐Ala‐OMe (II), Ala‐Arg‐Glu‐Lys‐Ala‐OMe (III), and Ala‐Arg‐Ala‐Lys‐Ala‐OMe (IV) as well as the conditions for the removal of the protecting groups is presented. Gel III contains the natural peptide sequence Arg‐Glu‐Lys while the other gels are analogs of this sequence.