Construction of a dimeric DNA-binding peptide model by peptide-anthraquinone conjugation.
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.
Takenaka
S
S
Department of Chemical Science and Technology, Kyushu University, Fukuoka, Japan.
Sato
H
H
Itakura
Y
Y
Kondo
H
H
Takagi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000880:Anthraquinones / Q000737:chemistry*; D001483:Base Sequence; D002417:Cattle; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry*; D008024:Ligands; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011494:Protein Kinases / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins
D000880:Anthraquinones; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D008024:Ligands; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; D004247:DNA; D011494:Protein Kinases