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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 indicatingdoi:10.5281/zenodo.2559215 fatcat:qadyfaqugzcgpnmjqryuzkiiqi