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Construction of a dimeric DNA-binding peptide model by peptide-anthraquinone conjugation
S Takenaka1, H Sato, Y Itakura
1Department of Chemical Science and Technology, Kyushu University, Fukuoka, Japan.
International Journal of Peptide and Protein Research
|October 1, 1996
Abstract:
A peptide-anthraquinone conjugate was designed and synthesized containing linked peptide chains composed of Asp-Pro-Ala-Ala-Leu-Lys-Arg-Ala-Arg-Asn-Thr-Glu-Ala- Ala-Arg-Arg-Ser-Arg-Ala-Arg-Lys-Leu-Gln-Arg-Met, representing the basic region of GCN4. The two peptides were joined with anthraquinone at its 1- and 8-positions in a two-fold symmetric fashion, mimicking dimeric DNA-binding proteins. Experimental data indicated both an interaction of the anthraquinone moiety with the DNA double strand and an increase in the alpha-helicity of the peptide moieties of the ligand when it binds to DNA.