Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches

Abstract

The binding characteristics of indigotin with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by various spectroscopic techniques. Spectroscopic analysis revealed that the quenching mechanism between indigotin and HSA/BSA belonged to the static quenching. The displacement experiments suggested that indigotin primarily bound to tryptophan residues on proteins within site I. The thermodynamic parameters indicated that the binding of indigotin–HSA/BSA mainly depended on the hydrophobic interaction. The binding distance of indigotin to HSA/BSA was evaluated. The results by synchronous fluorescence, three-dimensional fluorescence, Fourier Transform Infrared spectroscopy (FT-IR) and circular dichroism (CD) spectra showed that the conformation of proteins altered in the presence of indigotin.

α-Glucosidase inhibitors from Chinese bayberry (Morella rubraSieb. et Zucc.) fruit: molecular docking and interaction mechanism of flavonols with different B-ring hydroxylations

“…Since correlation coefficients (R b ) were all above 0.99, assumption underlying the derivation of eqn (6) was reasonable. 61 Since values of n were all approximately equal to 1 (Table 2), there was just one binding site on a-glucosidase in the presence of each avonol. It was consistent with the results obtained from Lineweaver-Burk plot analysis.…”

Spectroscopic and molecular modeling study of cyanine dye interacting with human serum transferrin

“…8. As evident from the figure, the CD spectra of free Tf exhibited two negative peaks at 208 and 220 nm, which were characteristic of the typical ␣-helix structure of proteins [30]. The reasonable explanation was that the negative peaks near 208 and 222 nm are both contributed by n → * transfer for the peptide bond of ␣-helix [31].…”

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

“…It suggests that the interaction of Cu(II) ions with BSA and HSA affects the conformation of tryptophan microregion only. 55 …”

“…It suggests that the interaction of Cu(II) ions with BSA and HSA affects the conformation of tryptophan microregion only. 55 Influence of Cu(II) Ions on Oligomerization, Aggregation, and Amyloid Fibril Formation in the Case of Serum Albumins. The Cu(II) ion concentration-dependent nanoscale morphological changes of serum albumins in aqueous solution were investigated using tapping mode AFM and compared with that of pure proteins.…”