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Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: A FRET study

Paper ID Volume ID Publish Year Pages File Format Full-Text
29747 44434 2011 6 PDF Available
Title
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.

Graphical abstractPicosecond resolved Förster resonance energy transfer (FRET) from warfarin to rifampicin at various binding sites of the transporter protein HSA has been shown. The schematic representation of the FRET pathway from the single tryptophan (Trp214) to the nearby warfarin has also been shown.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The complex structure of antibiotics against the diseases tuberculosis, Rifampicin with Human serum protein has been explored. ► Picosecond resolved FRET from an anti-thrombosis drug, warfarin to rifampicin explores possible binding sites of rifampicin on the protein. ► The structural consequence of simultaneous binding of the two important drugs in the plasma proteins has also been explored. ► The potential problem of using intrinsic tryptophan as an FRET donor in the above studies has also been discussed.

Keywords
Rifampicin; Warfarin; Binding interaction with transporter protein; FRET; TCSPC; CD
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Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: A FRET study
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 103, Issue 2, 3 May 2011, Pages 153–158
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us