Any changes in protein normal conformation and configuration can lead to toxic aggregation events andproduce conformational diseases[1,2]. Regards to widespread usage of potassium sorbate(PS) and sodiumbenzoate(SB) in nowadays human life style and their possible risks, we studied the effect of them onhuman serum albumin structural changes and their interference with Maillard reaction in presence andabsence of glucose during some incubation time. All of these studies were done via biophysicaltechniques including fluorescence and circular dichroism spectroscopy (CD), differential scanningcalorimetry (DSC), AFM, surface tension, molecular docking and LIGPLOT studies. TNBSA assayshowed that both of SBand PS had binding potential to HSA Lys residues through covalent bonds,triggered diabetes and formed glycotoxins especially PS. The docking and LIGPLOT studies revealed twodifferent physical interaction sites between HSA–PS/SB.The DSC results demonstrated different HSAenergetic domains and intermediate formation due to HSA incubation with PS or SB with or withoutglucose[3,4]. CD demonstrated the main differences in HSA secondary elements(helicity via SB or β-sheet via PS). The Th T and AFM resuls showed significant impact of PS on different amyloid fibrilformation with or without glucose than SB.The surface tension confirmed the destructive effect of PSon HSA structure than glucose. Also we see that some natural products (3-β- hydroxybutyrate andellagic acid)can inhibit the AGEs and fibril formation due to glucose and PS. This report shows areview on HSA aggregation via above oxidative reagents and outline how to inhibit the aggregation byantioxidants.