It has been demonstrated that coupling a host-guest complex formation onto the DNA binding ability of short peptides gave raise a cooperative DNA binding by short peptide dimers. This strategy was extend to study the DNA binding by oligomers of short peptide. An amino acid bearing the adamantyl group was incorporated at the N-terminal of a peptide derived from the basic region of a yeast transcription activator GCN4, and beta-cyclodextrin was attached at the C-terminal cysteine residue in the same peptide chain. DNA binding of the peptide with both host and guest molecules to tandemly repeated DNA sequences was studied by gel shift assay.