Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin

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

Kheirdoosh F¹ ; Kashanian S^{1, 2} ; Khodaei MM¹ ; Sariaslani M³ ; Falsafi M⁴ ; Moghadam NH⁵ ; Salehzadeh S⁶ ; Pazhavand M¹ ; Kashanian M⁷

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1. Department of Applied Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran
2. Nano drug delivery research center, Kermanshah University of medical sciences, Kermanshah, Iran
3. School of Paramedical, Kermanshah University of Medical Science, Kermanshah, Iran
4. Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran
5. Research Center for Molecular Medicine, Hamadan University of Medical Sciences, Hamadan, Iran
6. Faculty of Chemistry, Bu-Ali Sina University, Hamedan, Iran
7. School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran

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.

Style	Citing Format
MLA	Kheirdoosh F, et al.. "Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin." Nucleosides, Nucleotides and Nucleic Acids, vol. 40, no. 3, 2021, pp. 300-316.
APA	Kheirdoosh F, Kashanian S, Khodaei MM, Sariaslani M, Falsafi M, Moghadam NH, Salehzadeh S, Pazhavand M, Kashanian M (2021). Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin. Nucleosides, Nucleotides and Nucleic Acids, 40(3), 300-316.
Chicago	Kheirdoosh F, Kashanian S, Khodaei MM, Sariaslani M, Falsafi M, Moghadam NH, Salehzadeh S, Pazhavand M, Kashanian M. "Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin." Nucleosides, Nucleotides and Nucleic Acids 40, no. 3 (2021): 300-316.
Harvard	Kheirdoosh F et al. (2021) 'Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin', Nucleosides, Nucleotides and Nucleic Acids, 40(3), pp. 300-316.
Vancouver	Kheirdoosh F, Kashanian S, Khodaei MM, Sariaslani M, Falsafi M, Moghadam NH, et al.. Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin. Nucleosides, Nucleotides and Nucleic Acids. 2021;40(3):300-316.
BibTex	@article{ author = {Kheirdoosh F and Kashanian S and Khodaei MM and Sariaslani M and Falsafi M and Moghadam NH and Salehzadeh S and Pazhavand M and Kashanian M}, title = {Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin}, journal = {Nucleosides, Nucleotides and Nucleic Acids}, volume = {40}, number = {3}, pages = {300-316}, year = {2021} }
RIS	TY - JOUR AU - Kheirdoosh F AU - Kashanian S AU - Khodaei MM AU - Sariaslani M AU - Falsafi M AU - Moghadam NH AU - Salehzadeh S AU - Pazhavand M AU - Kashanian M TI - Spectroscopic Studies on the Interaction of Aspartame With Human Serum Albumin JO - Nucleosides, Nucleotides and Nucleic Acids VL - 40 IS - 3 SP - 300 EP - 316 PY - 2021 ER -

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