Abstract
Albumin is one of the most important proteins in human blood. Among its multiple functions, drug binding is crucial in terms of drug distribution in human body. This protein undergoes many modifications that are certain to influence protein activity and affect its structure. One such reaction is albumin oxidation. Chloramine T is a strong oxidant. Solutions of human serum albumin, both non-modified and modified by chloramine T, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. 10H-3,6-diazaphenothiazine (DAPT) has anticancer activity and it has been studied for the first time in terms of binding with human serum albumin—its potential as a transporting protein. Using fluorescence spectroscopy, in the presence of dansylated amino acids, dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), DAPT binding with two main albumin sites—in subdomain IIA and IIIA—has been evaluated. Based on the conducted data, in order to measure the stability of DAPT complexes with human (HSA) and oxidized (oHSA) serum albumin, association constant (Ka) for ligand-HSA and ligand-oHSA complexes were calculated. It has been presumed that oxidation is not an important issue in terms of 10H-3,6-diazaphenothiazine binding to albumin. It means that the distribution of this substance is similar regardless of changes in albumin structure caused by oxidation, natural occurring in the organism.
Highlights
Human serum albumin (HSA) is the most important protein in plasma [1]
Has induced bothstress intracellularly and stress extrahas been linked to a number of chronic diseases
Several of oxidation indicate that the changes serum as one of themodels main substances transporting exogenous and in structure and activity of oxidized proteins affect the binding properties ażekendogenous compounds, affects the bioavailability of many drugs
Summary
Human serum albumin (HSA) is the most important protein in plasma [1]. HSA plays various functions in the human body. It is 70% responsible for maintaining oncotic pressure [2]. Albumin has the ability to bind both exo- and endogenous substances and is an important element in the distribution of drugs in the human body. Binding to albumin may increase the half-life of drugs, reduce drug toxicity, increase solubility and protect against oxidation [3,4]. Protein properties allow for its numerous applications in medicine
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