Investigation of influence of different values of pH on mechanisms of binding of human serum albumin with markers of fluorescein family

Objective and background data ork is dedicated to investigation of influence of different values of pH on mechanisms of binding of human serum albumin (HSA) with markers of fluorescent family – eosin, erythrosin and fluorescein. For this purpose were detected changes in markers fluorescence, in markers molecular association, in the effective constants of binding of markers to HSA and also in changes in related chemical bonds in HSA-marker association. Such analysis of changes in binding of biomolecules (such as proteins) with different ligands (such as markers) is extremely interesting from the point of view of a biomedicine and pharmaceuticals, so from the point of view of bionanotechnology: for example, at creation of new drugs. s vestigations of steady-state fluorescence, polarized fluorescence, molecular association of markers of fluorescein family in HSA solutions are presented in this work, also the analysis of changes in related chemical bonds in HSA-marker association by Raman spectroscopy is done, and also the effective constants of binding of markers to HSA are calculated. s and conclusion vestigations show the leading role of chemical and electrostatic interactions between markers and HSA. The received data allow one to get information about mechanisms of interaction of markers to HSA, that can be useful at research of structure and properties of binding Centers (drug-binding Centers) of transport blood protein–HSA, what is of great importance in medical investigations of binding of drugs to HSA.