Interaction Between 2′,4-Dihydroxychalcone and the N, F, E Conformers of Bovine Serum Albumin: Influence of Temperature and Ionic Strength

• Published in: The Protein Journal 2012-04, Vol.31 (4), p.293-299
• Main Authors: Curvale, Rolando A., Debattista, Nora B., Pappano, Nora B.
• Format: Article
• Language: English
• Subjects: Albumin; Analysis; Animal Anatomy; Animals; Binding Sites; Biochemistry; Biological properties; Bioorganic Chemistry; Cattle; Chalcones - chemistry; Chalcones - metabolism; Chemistry; Chemistry and Materials Science; Electrolytes; Histology; Kinetics; Molecular Structure; Morphology; Organic Chemistry; Osmolar Concentration; Protein Binding; Proteins; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Spectrum analysis; Temperature; Temperature effects; Thermodynamics; Ultraviolet spectroscopy
• ISSN: 1572-3887; 1573-4943; 1875-8355
• DOI: 10.1007/s10930-012-9404-y

UV–Vis spectroscopy was used to study the interaction between the 2′,4- dihydroxychalcone, flavonoid which is known to have anti-tumor activity in vitro, and others biological properties, and the N, F and E conformers of bovine serum albumin at different ionic strengths and temperatures. The Klotz model was found to be adequate to determine the constants and number of binding sites. The reaction was found to be exothermic and spontaneous. The number of binding sites decreases and the reaction is more exergonic along with the increase in ionic strength and the conformational change of N to E. The reactions were necessarily hydrophobic and followed by a process of ionic character.