Carbohydrate-minor groove interactions in the binding of calicheamicin gamma1(super I) to duplex DNA

The binding affinity between calicheamicin and a single TCCT.AGGA site within a synthetic duplex DNA is measured by kinetic analysis. DNA binding affinity of the carbohydrate domain is analyzed by competitive binding analysis involving calicheamicin and the calicheamicin oligosaccharide. Iodine substituent on the aromatic ring of the carbohydrate domain interacts with the exocyclic C2-NH2 group or both guanine residues at the target site.