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Updated: Jun 14, 2026

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
Published on: August 20, 2012
A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin
Paulami Mandal1, Munmun Bardhan, Tapan Ganguly
1Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700 032, India.
Abstract:
UV-vis, time-resolved fluorescence and circular dichroism spectroscopic investigations have been made to reveal the nature of the interactions between xanthene dye Rhodamine 6G and the well known protein hemoglobin. From the analysis of the steady-state and time-resolved fluorescence quenching of Rhodamine 6G in aqueous solutions in presence of hemoglobin, it is revealed that the quenching is static in nature. The primary binding pattern between Rhodamine and hemoglobin has been interpreted as combined effect of hydrophobic association and electrostatic interaction. The binding constants, number of binding sites and thermodynamic parameters at various pH of the environment have been computed. The binding average distance between the energy donor Rhodamine and acceptor hemoglobin has been determined from the Forster's theory.
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