A novel family of glycopolythiophenes containing sialic acid or mannose ligands were prepared and evaluated for their ability to bind lectins, virus, and bacteria. For the set of glycopolythiophenes studied, the spacer-length between the polymer backbone and the ligand was varied to optimize binding interactions. The glycopolymers were blue-shifted (absorbance of ca. 400 nm) relative to the corresponding homo-polythiophenes (absorbance ca. 440 nm), suggesting a twisted conformation for the glycopolymers. The altered conformation is likely due to electrostatic or H-bonding interactions between the polymer chains, arising from the carbohydrate ligand. Further conformational changes in the polythiophene backbone were detected by the binding of specific receptors; lectins (wheat germ agglutinin, concanavalin A), Influenza virus, and Escherichia coli. The binding interactions result in an unusual red-shift in the visible absorption of the polymer backbone, suggesting a lengthening of the effective conjugated length upon interaction of the ligand with its congnate receptor. These conjugated glycopolymeric systems offer a potentially new platform for the detection of molecular binding interactions.