Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: A FRET study
| Autor: | Abhinandan Makhal, Priya Rajdev, Tanumoy Mondol, Samir Kumar Pal |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Drug
Circular dichroism media_common.quotation_subject Antitubercular Agents Biophysics Fibrinolytic Agents Fluorescence Resonance Energy Transfer medicine Humans Radiology Nuclear Medicine and imaging Binding site Protein secondary structure Serum Albumin media_common Radiation Radiological and Ultrasound Technology Chemistry Circular Dichroism Tryptophan Human serum albumin Transport protein Förster resonance energy transfer Biochemistry Warfarin Rifampin medicine.drug |
| Zdroj: | Journal of Photochemistry and Photobiology B: Biology. 103:153-158 |
| ISSN: | 1011-1344 |
| DOI: | 10.1016/j.jphotobiol.2011.02.023 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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