Comparative Studies on the Interaction Between Bovine β-lacto-globulin Type A and B and a New Designed Pd(II) Complex with Anti-tumor Activity at Different Temperatures
| Autor: | Ali Akbar Saboury, Faizan Ahmad, Mahboube Islami Moghaddam, Adeleh Divsalar, H. Mansoori-Torshizi, Golam Hossein Hakimelahi |
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| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Quenching (fluorescence) biology medicine.diagnostic_test Chemistry Analytical chemistry General Medicine Binding constant Fluorescence spectroscopy Hydrophobic effect Crystallography Structural Biology Spectrophotometry biology.protein Proton NMR medicine Molecular Biology Beta-lactoglobulin |
| Zdroj: | Journal of Biomolecular Structure and Dynamics. 26:587-597 |
| ISSN: | 1538-0254 0739-1102 |
| Popis: | An new water-soluble Pd(II) complex, 2,2'-bipyridin n-butyl dithiocarbamato Pd(II) nitrate has been synthesized. The Pd(II) complex has been characterized by elemental analysis and conductivity measurements as well as spectroscopic methods such as infrared, 1H NMR, and ultraviolet-visible. The interaction between this new design Pd(II)-complex, an anti-tumor component, with carrier proteins of β-lactoglobulin-A and -B (BLG-A and -B) were studied at different temperatures of 27, 37, 42, and 47 °C by fluorescence spectroscopy and far-UV circular dichroism (CD) spectrophotometric techniques. A strong fluorescence quenching interaction of Pd(II) complex with BLG-A and -B was observed at different temperatures. The binding parameters were evaluated by fluorescence quenching method. The thermodynamic parameters, including ΔH°, ΔS°, and ΔG° were calculated by fluorescence quenching method indicated that the electrostatic and hydrophobic forces might play a major role in the interactions of Pd(II) complex with BLG-A and -B, respectively. The distances between donors (Trps of the BLG-A and -B) and acceptor (Pd(II) complex) were obtained according to the fluorescence resonance energy transfer (FRET). Far-UV CD studies showed that the Pd(II) complex did not represent any significant changes in the secondary structures of BLG- A and -B. The difference in the interaction properties observed for BLG-A and -B with Pd(II) complex is related to the difference in the amino acid sequences between these two variants. |
| Databáze: | OpenAIRE |
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