Isfahan University of Medical Sciences

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Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin Publisher Pubmed



Kheirdoosh F1 ; Kashanian S1, 2 ; Khodaei MM1 ; Sariaslani M3 ; Falsafi M4 ; Moghadam NH5 ; Salehzadeh S6 ; Pazhavand M1 ; Kashanian M7
Authors

Source: Nucleosides, Nucleotides and Nucleic Acids Published:2021


Abstract

In this work the binding of artificial sweetener aspartame with human serum albumin (HSA) was studied at physiological pH. Binding studies of aspartame (APM) with HSA are useful to understand APM -HSA interaction, mechanism and providing guidance for the application and design of new and more efficient artificial sweeteners. The interaction was investigated by spectrophotometric, spectrofluorometric competition experiment and circular dichroism (CD) techniques. The results indicated that the binding of APM to HSA caused fluorescence quenching of HSA through static quenching mechanism with binding constant 1.42 × 10+4 M−1 at 298 K and the number of binding sites is approximately one. Thermodynamic parameters, enthalpy changes (ΔH) and entropy changes (ΔS) were calculated to be −41.20 kJ mol−1 and −58.19 J mol−1 K−1, respectively, according to van’t Hoff equation, which indicated that reaction is enthalpically driven. Quenching of the fluorescence of HSA was found to be a static quenching process. The binding constants and number of binding sites were obtained at three different temperatures (298, 308 and 318 K). Combining above results and those of spectrofluorometric competition experiment and circular dichroism (CD), indicated that APM binds to HSA via Sudlow’s site I. Furthermore, the study of molecular docking on HSA binding also indicated that APM can strongly bind to the site I (subdomain IIA) of HSA mainly by hydrophobic interaction and hydrogen bond interactions exist between APM and HSA. © 2021 Taylor & Francis Group, LLC.