Spectroscopic and nano-molecular modeling investigation on the binary and ternary bindings of colchicine and lomefloxacin to Human serum albumin with the viewpoint of multi-drug therapy

Spectroscopic and nano-molecular modeling investigation on the binary and ternary bindings of colchicine and lomefloxacin to Human serum albumin with the viewpoint of multi-drug therapy

Combination of several drugs is often necessary especially during long-term therapy. The competitive binding drugs can cause a decrease in the amount of drug bound to protein and increase the biological active fraction of the drug. The aim of this study is to analyze the interactions of Lomefloxacin...

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Bibliographic Details
Published in:Journal of luminescence Vol. 130; no. 12; pp. 2476 - 2486
Main Authors: Chamani, J., Asoodeh, A., Homayoni-Tabrizi, M., Amiri Tehranizadeh, Z., Baratian, A., Saberi, M.R., Gharanfoli, M.
Format: Journal Article
Language:English
Published: Amsterdam Elsevier B.V 01-12-2010
Elsevier
Subjects:
Binary systems
Binding
Biological and medical sciences
Colchicine
Drugs
Fluorescence
Fundamental and applied biological sciences. Psychology
HSA
Interactions. Associations
Intermolecular phenomena
Lomefloxacin
Molecular biophysics
Molecular dynamic
Nanostructure
Proteins
Spectroscopy
Ternary systems
Therapy
Spectroscopy
Colchicine
HSA
Lomefloxacin
Molecular dynamic
Human
Light scattering
Molecular dynamics method
Fluorescence
Serum albumin
Conformational changes
Protein
Circular dichroism
Binding energy
Luminescence quenching
Synchrotron radiation
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Summary:Combination of several drugs is often necessary especially during long-term therapy. The competitive binding drugs can cause a decrease in the amount of drug bound to protein and increase the biological active fraction of the drug. The aim of this study is to analyze the interactions of Lomefloxacin (LMF) and Colchicine (COL) with human serum albumin (HSA) and to evaluate the mechanism of simultaneous binding of LMF and COL to protein. Fluorescence analysis was used to estimate the effect of drugs on the protein fluorescence and to define the binding and quenching properties of drugs-HSA complexes. The binding sites for LMF and COL were identified in tertiary structure of HSA with the use of spectrofluorescence analysis. The analysis of fluorescence quenching of HSA in the binary and ternary systems show that LMF does not affect the complex formed between COL and HSA. On the contrary, COL decreases the interaction between LMF and HSA. The results of synchronous fluorescence, resonance light scattering and circular dichroism spectra of binary and ternary systems show that binding of LMF and COL to HSA can induce micro-environmental and conformational changes in HSA. The simultaneous presence of LMF and COL in binding to HSA should be taken into account in the multi-drug therapy, and necessity of using a monitoring therapy owning to the possible increase of the uncontrolled toxic effects. Molecular modeling of the possible binding sites of LMF and COL in binary and ternary systems to HSA confirms the spectroscopic results.
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content type line 23
ISSN:0022-2313
1872-7883
DOI:10.1016/j.jlumin.2010.08.016