Interaction between the anti-cancer drug diacetyl maslinic acid and bovine serum albumin: A biophysical study
| Autor: | J.A. Molina-Bolívar, Andrés Parra, M. Medina-O´ Donnell, C. Carnero Ruiz, Francisco Galisteo-González |
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| Rok vydání: | 2015 |
| Předmět: |
biology
Stereochemistry Enthalpy Intermolecular force Condensed Matter Physics Fluorescence Atomic and Molecular Physics and Optics Electronic Optical and Magnetic Materials Hydrophobic effect chemistry.chemical_compound chemistry Maslinic acid Materials Chemistry biology.protein Biophysics Molecule Physical and Theoretical Chemistry Bovine serum albumin Protein secondary structure Spectroscopy |
| Zdroj: | Journal of Molecular Liquids. 208:304-313 |
| ISSN: | 0167-7322 |
| DOI: | 10.1016/j.molliq.2015.04.050 |
| Popis: | Steady-state and time-resolved fluorescence, as well as Fourier transform-infrared (FT-IR) spectroscopy studies were made to understand the interaction between diacetyl maslinic acid (DMA) and bovine serum albumin (BSA) at pH 7.4. A decrease in fluorescence intensity and a blue shift of the emission peak were observed in the DMA–BSA complex, which were attributed to changes in the microenvironment of the protein fluorophores. Spectroscopic analysis revealed that the fluorescence-quenching mechanism between DMA and BSA was a static procedure. Displacement experiments with site markers indicated that DMA binds to BSA at Sudlow's site I (subdomain IIA). Binding constants for the protein–drug interaction were determined at three different temperatures (298, 305, and 310 K). Enthalpy (ΔH0) and entropy (ΔS0) changes indicated that hydrophobic interactions were the dominant intermolecular forces in the binding of DMA to BSA. The interaction appears to be entropy-driven, and the process spontaneous and endothermic. Enthalpy–entropy compensation suggests that reorganization of water molecules plays an important role. Anisotropy and FT-IR experiments revealed that BSA loses its structure in the presence of DMA. The secondary structure compositions of free BSA and DMA–BSA complex were determined by FT-IR. The binding distance and transfer efficiency for DMA–BSA complex were calculated according to the Foster theory of non-radiative energy transfer. |
| Databáze: | OpenAIRE |
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