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Authors
Affiliations
1 Department of Biophysics, Molecular Biology and Bioinformatics, University College of Science, University of Calcutta,
92 Acharyya Prafulla Chandra Road, Kolkata 700 009, IN
Source
Current Science, Vol 108, No 3 (2015), Pagination: 364-371
Abstract
This study investigates interaction of glycyrrhizin (an herbal therapeutic agent) with human haemoglobin. The interaction is confirmed by glycyrrhizin-induced quenching of absorbance and fluorescence data. Both hydrophobic and electrostatic interactions appear to be involved in glycyrrhizin-haemoglobin binding. The binding causes no change in the secondary structure of haemoglobin. The interaction decreases H2O2- induced iron release from haemoglobin and haemoglobin- mediated oxidative reactions. Glycyrrhizin inhibits ferryl-haemoglobin formation, peroxidase and esteraselike activities of the heme protein. Almost no oxygen is released from haemoglobin due to glycyrrhizin binding. The interaction thus reduces haemoglobin-mediated oxidative damage without affecting oxygen-binding capacity of the protein, and may be an advantage in therapeutic application of glycyrrhizin.
Keywords
Free Iron, Glycyrrhizin, Haemoglobin, Oxidative Stress.
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