Effect of metal ions on the interaction between bovine serum albumin and berberine chloride extracted from a traditional Chinese Herb coptis chinensis franch

Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin

“…The molecular interactions between proteins and many compounds have been investigated successfully including dyes and other some organic small molecules [3,[5][6][7][8][9][10]. However, the binding of some inorganic ions to proteins has seldom been investigated [11,12].…”

Biological Evaluation of a New Synthesized Pt(II) Complex by Cytotoxic and Spectroscopic Studies

“…We have utilized the following equation (Eq. 2) for investigating the binding parameters upon the addition of Pt(II) complex to b-CN, describing the quenching phenomenon of the fluorescence emission [34].…”

Investigation of effects of newly synthesized Pt(II) complex against human serum albumin and leukemia cell line of K562

“…Tryptophan 214 fluorescence is the most frequently examined among the three intrinsic aromatic fluorophores in HSA molecules to obtain information about conformational changes of the protein (21). The intrinsic fluorescence of the HSA at different temperatures (27,37,42 and 47 o C) at 335 nm with varying concentrations of Pt(II) complex are represented in Fig. 2.…”

“…Therefore, the dependence of thermodynamic parameters on the temperature was analyzed in order to further characterize the acting forces between Pt(II) complexes and HSA. The acting forces between a small molecule and macromolecule include hydrogen bond, Van der Waals force, electrostatic force, hydrophobic interaction force, and so on (25)(26)(27). The thermodynamic binding parameters of enthalpy change (ΔH o ) and entropy change (ΔS o ) were determined using van't Hoff equation (23): …”

“…The excitation wavelength was adjusted at 280 nm and the emission spectra were recorded for all of the samples at different temperatures (27,37,42 ) based on a mean amino acid residue weight of 113.7 (MRW). The molar ellipticity was determined as [θ]λ= (100 × MRW × θobs/cl), where θobs is the observed ellipticity in degrees at a given wavelength, c is the protein concentration in mg/ml and l is the length of the light path in mm.…”