A novel approach of interaction between bilirubin and human serum albumin in the presence of Aspirine

Abstract

Introduction: Bilirubin (BR), the yellow neurotoxic pigment of jaundice and the end product of heme metabolism in mammals, is lipophilic tetrapyrrole dicarboxylic acid. Human serum albumin (HSA) is a principal extra cellular protein. Its primary pharmacokinetics function is participating in absorption, distribution, metabolism and excretion of drug. Acetylsalicylic acid (ASA) has been shown to reduce the risk for colorectal cancer by as much as approximately 40%, a property that is shared by other nonsteroidal anti-inflammatory drugs. Materials and methods: BR, ASA and HSA were purchased from Sigma. Fluorescence measurements were carried out on a F-2500. Molecular modeling was done by autodock software. Result and discussion: Investigating the interaction of drugs to HSA can elucidate the properties of drug–protein complex. Synchronous fluorescence spectroscopy from the interaction of HSA with BR and in the presence of Aspirin showed that ligand affect the conformation of HSA. Interaction of BR and ASA with HSA changed the binding affinity of second drug that can use the location in the binding site on protein. On the other hand we found that the binding affinity of ASA bound to HAS was stronger in the presence of BR, and considered the same result for addition of ASA to HAS-BR complex.