Thermodynamic studies on the interaction of folic acid with bovine serum albumin

An investigation of folic acid–protein association sites and the effect of this association on folic acid self-assembly

“…Therefore, BSA forms a blue dye-BSA complex that can be detected by a UV-Vis spectrophotometer at 595 nm [22]. However, FA and BSA also form complexes with each other [16,17]. Note that dye-BSA complexes continue to form even after FA-BSA association (as recorded in the spectrographs shown in Fig.…”

“…FA forms complexes with proteins such as bovine serum albumin (BSA) and human serum albumin (HSA) [16] due to electrostatic forces and hydrogen bonding [17]. Most of the studies focused to increase the bioavailability of FA and used spectroscopic techniques to probe the interactions between FA and BSA.…”

“…Most of the studies focused to increase the bioavailability of FA and used spectroscopic techniques to probe the interactions between FA and BSA. According to the literature, tryptophan (Trp) can be involved in FA-protein associations [16,17]. Moreover, Trp itself forms a complex with FA [18].…”

Energetics of albumin-disuccinylmaslinic acid binding determined by fluorescence spectroscopy

“…These factors contribute to the affinity constant and energetic of the binding process. The influence of electrolyte on this constant is often used to assess the role of electrostatic interaction on the association process [27], as an increase in electrolyte concentration reduces the contribution of this interaction to the binding of Gibbs energy and thus weakens binding. Our results suggest that electrostatic interactions contribute to SMA-BSA binding, since they are screened by the presence of NaCl in the medium.…”

Thermodynamics of aromatic amino acid interactions with heterocyclic ligands

“…Of great importance in pharmacology, supramolecular chemistry and physical chemistry are the study of binding drugs to proteins [1][2][3][4][5]. It is well known that amino acids are building blocks of proteins.…”