H. Eckstein, H. Schott
Dec 1, 1980
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Journal
Macromolecular Chemistry and Physics
Abstract
The syntheses of models of histones are described. The lysine derivative Ne-Boc-lysine methylester, the protected peptides (Lys(Z))5,(Lys(Boc))5-Pro-OtBu and the protected sequence 17–27 of the histone H1 of rabbit thymus, Pro-Ala-(Lys(Boc))4-Ala-Ala-(Lys(Boc))2-Pro-OMe, were transferred via three different ways into insoluble gels. The first synthetic way started with acrylamides, obtained by the reaction of the active benzotriazol-1-yl acrylate (3) with Nα-amino groups of the lysine derivative and of derivatives of lysine peptides. The acrylic peptides were copolymerized with tetramethylene dimethacrylate and thus transferred into insoluble gels. In a second way partially protected peptides were coupled with carboxylic groups of cross-linked polyacrylic gels. The third way followed the principle of the solid phase peptide synthesis. Cleavage of the protecting groups resulted in lysine and lysine peptide gels, which resemble different models of histones. The peptide gels can be used both for column chromatographic investigations of the peptide-nucleotide interaction and for affinity-chromatography.