Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: A FRET study
Abstract
Although rifampicin (Rf) is one of the most effective antibiotics against infection caused by Mycobacterium tuberculosis, interaction of the drug with universal carrier protein in human blood plasma is not fully understood. Reduction of medicinal efficacy of other drugs, including anti-thrombosis drug warfarin (Wf), to the patients on Rf therapy also needs molecular understanding. In the present work we have studied interaction of Rf with one of the model carrier protein (human serum albumin). By using circular dichroism (CD) spectroscopy we have characterized the change in the secondary structure of the protein. The consequence of the simultaneous binding of the two drugs, Rf and Wf, on the structure of the protein has also been explored. Picosecond resolved Förster resonance energy transfer (FRET) from Wf to Rf explores possible binding sites of the anti-tuberculosis drug on the protein. In this report, we have discussed the potential problem of using the single tryptophan of the protein (Trp 214) as energy donor in FRET experiment for the characterization of the binding site of the drug Rf on the protein.
Additional Information
© 2011 Elsevier B.V. Received 24 October 2010; revised 25 February 2011; accepted 28 February 2011. Available online 5 March 2011. AM wants to thank CSIR for the fellowship. We thank DST, India for the financial grant (SR/SO/BB-15/2007).Additional details
- Eprint ID
- 23714
- Resolver ID
- CaltechAUTHORS:20110518-111000808
- CSIR Fellowship
- SR/SO/BB-15/2007
- DST (India)
- Created
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2011-05-18Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field