A Spectroscopic Study of the Interaction between Cyanine Dyes with Different Skeleton Structures and Transferrin

Human serum transferrin (hTf) has been exploited as a bio-carrier for targeted drugs to cancer cells where transferrin receptors are expressed at high levels. In this study, cyanine dyes DMSA and DMSB with a similar main core structure were selected to evaluate the effects of heterocycle on binding with hTf by spectroscopic methods. Fluorescence spectral results have shown that DMSB, which contains a selenazole ring, had a strong affinity binding with transferrin, up to 10(4)-fold higher than DMSA, which contains a thiazole ring. This difference may be attributed to the larger molecular volume of selenazole compared with DMSA. Binding distance between cyanine dyes and hTf demonstrated that the non-radioactive energy transfer mechanism was also involved in the fluorescence quenching of protein. Furthermore, DMSB-binding gave rise to a greater decrease of the alpha-helix content of hTf than DMSA suggesting that hTf, which shows a looser structure binding with DMSB, increased polarity around the tryptophan residues of hTf, which was confirmed by circular dichroism and synchronous fluorescence spectroscopy. The study provides a certain theoretical basis for the design of cyanine dyes as biomolecular probe to target drugs for hTf.