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INTERACTION OF ANTI MERS-COV RIBAVIRIN WITH HUMAN SERUM ALBUMIN IN DISEASE MIMETIC CONDITIONS OF DIABETES AND UREMIA AN IN-VITRO STUDY

AFahad M Almutairi*, Mohammad Rehan Ajmal

The binding characteristics of ribavirin to human serum albumin (HSA) have been studied using fluorescence technique under in vitro disease mimetic conditions of uremia and diabetes. Ribavirin is found to bind moderately (Kb-104) with glycated and native HSA. There is decrease in binding both in glycated human serum albumin and with human serum albumin in presence of urea. Ribavirin binding leads to intrinsic fluorescence quenching of HSA, glycated albumin and HSA in presence of urea indicating ribavirin binding to transport protein. Binding constant values decreased with increasing temperatures suggesting the quenching mode operating in the binding interaction of ribavirin with HSA and GHSA is static. Binding process was found to be spontaneous and exothermic. Analysis of the quenching and thermodynamic parameters of protein ligand system suggested the change in intermolecular interactions between ribavirin and HSA upon protein modification by glycation and in presence of urea leading to loss in ligand binding. Keywords: Glycated human serum albumin; uremia; fluorescence spectroscopy; ligand binding; ribavirin

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