Isothermal titration calorimetry investigation of the interactions between vitamin B6-derived hydrazones and bovine and human serum albumin

Abstract The binding of low molecular weight compounds with the transport proteins blood is an essential step their delivery into living cells and thus accurate investigation interactions occurring in solution at physiological conditions crucial for development efficient biologically active molecules. In this work, we report on complex species, stability constants thermodynamic parameters reactions hydrazones derived from pyridoxal-5ʹ-phosphate (PLP) bovine human serum albumin (BSA HSA) neutral aqueous solution. study has been carried out using isothermal titration calorimetry which allowed to directly obtain both constant enthalpy change values systems investigated. characterization revealed that PLP-hydrazone derivatives are able effectively interact enabled determination driving forces recognition process. formation 1:1 was found be always favored driven due insertion hydrazone moieties hydrophobic pockets BSA or HSA.