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Human Serum Albumin (HSA) is abundant plasma protein in human blood. It plays a critical role in the transport and distribution of endogenous and exogenous compounds. Protein binding affects free fraction of a drug thus affecting pharmacokinetics and therapeutic efficacy. Glycation of HSA under diabetic conditions and the accumulation of uremic toxins in uraemia may alter drug-protein interactions. Therefore, the present study aimed to investigate the binding interactions of ribavirin and selected uremic toxins with binding interactions involving glycation-sensitive HSA residues using molecular docking analysis. Molecular docking results demonstrated that ribavirin bind to HSA with hydrogen bonding and hydrophobic interactions. Key glycation-prone residues, including ARG222, ARG218, and LYS195, were identified at the ribavirin binding site. Several of these residues were also involved in the binding of uremic toxins, indicating potential competition for ligand binding in diabetic and uremic conditions. The overlap of interaction sites suggests that glycation and toxin accumulation may influence the structural and biochemical properties of HSA, thereby affecting ribavirin binding affinity and distribution. In conclusion, this study highlights the important role of glycation-sensitive HSA residues in mediating ribavirin and uremic toxin interactions. These insights may support the future design and optimization of ribavirin-based therapeutics.