Probing the interaction of human serum albumin with bilirubin in the presence of aspirin by multi-spectroscopic, molecular modeling and zeta potential techniques: insight on binary and ternary systems.

摘要: Here, we report on the effect of aspirin (ASA), binding parameters with regard to bilirubin (BR) human serum albumin (HSA). Two different classes sites were detected. Binding first and second was dominated by hydrophobic forces in case HSA-BR, whereas ternary system, achieved electrostatic interaction. The constant (K(a)) number site (n) obtained 1.6 × 10(6)M(-1) 0.98, respectively, for primary 3.7 0.84, presence ASA (ternary complex) at λ(ex)= 280 nm. progressive quenching protein fluorescence as BR concentration increased indicated an arrangement domain IIA HSA. Changes environment aromatic residues also observed synchronous spectroscopy (SFS). secondary structure HSA involving a decrease α-helical β-sheet contents amounts turns unordered conformations mainly found high concentrations BR. For time, relationship between structural HSA-BR RLS determining critical induced aggregation (C(CIAC)) absence investigated, there more significant enhancement mixture opposed binary one. zeta potential HSA-ASA complex demonstrated adsorption this anionic ligand onto surface system well both complex. By performing docking experiments, it that acting > hydrogen bonding interactions, consequently had long storage time blood plasma, especially ASA. This due interaction force being stronger (HSA-ASA) than In addition, that, ASA, altered, but did not become significantly modified, thus affinity barely changed without