Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Abstract

The temperature dependence of the interactions between some steroids (fusidic acid, ouabain and ethynodioldiacetate) and human serum albumin (HSA) at physiological pH (7.4) were studied systematically by square-wave voltammetry. Also, these interactions were proven by means of UV-Vis. absorption spectroscopy and FT-IR spectroscopy techniques. The interaction parameters (binding constants and stoichiometries) at temperature range of 297.5-312.5 K were determined from electrochemical data. It is worthy that the temperature has played a positive role on the interactions of fusidic acid with HSA; however it has negative effective on the interaction parameters of HSA with ouabain or ethynodioldiacetate.

Selenium Nanoparticles as Potential Drug-Delivery Systems for the Treatment of Parkinson’s Disease

“…As can be seen in Table , the temperature increase led to lower K values suggesting noncovalent interactions as the main driver of bonding of fluorophores to the SeNP surface. Unlike covalent interactions, weak noncovalent interactions tend to weaken at higher temperatures leading to the destabilization of SeNP–fluorophore complexes . Thermodynamic parameters (Δ H 0 , Δ S 0 , and Δ G 0 given in Table ) divulged the forces operating between SeNPs and fluorophores during their interaction.…”

“…Unlike covalent interactions, weak noncovalent interactions tend to weaken at higher temperatures leading to the destabilization of SeNP−fluorophore complexes. 55 Thermodynamic parameters (ΔH 0 , ΔS 0 , and ΔG 0 given in Table 4) divulged the forces operating between SeNPs and fluorophores during their interaction.…”