Appearance of advanced glycation end products (AGEs) is an importantfactor in the development ofvarious disorders such asAlzheimer’s disease, cataract, Diabetes, Parkinson’s disease and chronickidneydisease [1-2]. Hyperglycemic conditions when the bloodglucose goes above normal results in increasedflux of glucoseand its metabolic intermediates toward different pathwayscontributing to the formation ofhighly toxic pro-oxidants calledAGEs [1-3]. One of the main targets of these events are proteins whichare glycated at lysine and arginine residues [3-4]. The glycation induced changes in thesecondarystructure and conformation and drug binding ability of themolecular structure can bestudied.Currently, Molecular Dynamics simulations are extensively used in the study ofstructure,dynamics, and function of many biomacromolecules [2-3]. The present study employs experimentalmethods like UV-visible, Circular dichroism, Fluorescence and docking tools to investigate the changesoccurred in secondary and tertiary structures of the bovine serum albumin (BSA) together with itsinteractions with glucose, potassium sorbate, and sodium benzoate molecules. The two later molecules arewidely used in cosmetics, tooth pastes and food products as preservatives. Data showed that sodiumbenzoate is able to react with Lys residues in BSA via covalent bonds. Fluorescence spectroscopy resultsrevealed partial unfolding of BSA when incubated with sodium benzoate in the presence or absence ofglucose. The results showed that potassium sorbate shortens the glycation time for BSA. In addition,secondary and tertiary structural changes were also observed in different intervals of incubation withglucose in the presence or absence of each of potassium sorbate and sodium benzoate.