Polyphenol Interactions with Functional Proteins: A Molecular Docking Study

  • U. Malovytsia Department of Medical Physics and Biomedical Nanotechnologies, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine https://orcid.org/0000-0002-7677-0779
  • V. Trusova Department of Medical Physics and Biomedical Nanotechnologies, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine https://orcid.org/0000-0002-7087-071X
  • M. Thomsen AAU Energy, Aalborg University, Esbjerg, Denmark https://orcid.org/0000-0001-6805-7247
  • K. Vus Department of Medical Physics and Biomedical Nanotechnologies, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine https://orcid.org/0000-0003-4738-4016
  • O. Zhyntniakivska Department of Medical Physics and Biomedical Nanotechnologies, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine https://orcid.org/0000-0002-2068-5823
  • G. Gorbenko Department of Medical Physics and Biomedical Nanotechnologies, V.N. Karazin Kharkiv National University, Kharkiv, Ukraine https://orcid.org/0000-0002-0954-5053
DOI: https://doi.org/10.26565/2312-4334-2025-2-51
Keywords: Polyphenols, Serum albumin, Hemoglobin, Cytochrome c, Molecular docking

Abstract

Polyphenols, bioactive phytochemicals with anticancer, immunomodulating, antioxidative, anti-inflammatory, antimicrobial and many other favorable properties currently attract considerable attention due to their promising therapeutic potential. Biomolecular interactions of polyphenolic compounds, particularly, their association with physiologically important proteins may largely account for their biological effects. In the present study the molecular docking technique was employed to characterize the binding of curcumin (enol and keto forms), resveratrol, sesamin, salycilyc and gallic acids to the functional proteins such as serum albumin, hemoglobin (deoxy and oxy forms), cytochrome c (oxidized and reduced forms). It was found that all examined polyphenols possess the highest affinities for serum albumin and deoxyhemoglobin, while the lowest affinities are observed for cytochrome c. The analysis of the protein-ligand interfacial amino acid residues revealed that there exist specific amino acids with the highest occurrence frequency in the polyphenol binding sites among which are lysine, arginine and tyrosine.

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References

C. Weng, and G. Yen, Canc. Treat. Rev. 38, 76 (2012), https://doi.org/10.1016/j.ctrv.2011.03.001

T. Ozdal, E. Capanoglu, and F. Altay, Food Res. Int. 51, 954 (2013). https://doi.org/10.1016/j.foodres.2013.02.009

N. Poklar Ulrih, Crit. Rev. Food Sci. Nutr. 57, 2144 (2017). https://doi.org/10.1080/10408398.2015.1052040

F. Shahidi, and C. Dissanayaka, Food Prod. Process and Nutr. 5, 2 (2023). https://doi.org/10.1186/s43014-022-00121-0

A. Bennick, Crit. Rev. Oral Biol. Med. 13, 184-196 (2002). https://doi.org/10.1177/154411130201300208

P. Xue, G. Zhang, J. Zhang, and L. Ren, Curr. Protein Pept. Sci. 22, 217 (2021). https://doi.org/10.2174/1389203721666201109112220

V. de Freitas, and N. Mateus, Curr. Organ. Chem. 16, 724 (2012). https://doi.org/10.2174/138527212799958002

T. Raja, W. Raja, V. Duraipandiyan, S. Ignacimuthu, U. Janakiraman, and S. Packiam, Curr. Med. Chem. 30, 4032 (2023). https://doi.org/10.2174/0929867330666221202152540

T. Xu, J. Na, Q. Liu, G. Kuang, Q. Zhang, and Y. Zhao, Mater. Today Commun. 41, 110575 (2024). https://doi.org/10.1016/j.mtcomm.2024.110575

B. Giardina, I. Messana, R. Scatena, and M. Castagnola, Crit. Rev. Biochem. Mol. Biol. 30, 165 (1995). https://doi.org/10.3109/10409239509085142

Y. Ow, D. Green, Z. Hao, and T. Mak, Nat. Rev. Mol. Cell. Biol. 9, 532 (2008). https://doi.org/10.1038/nrm2434

S.J. Hewlings, and D.S. Kalman, Foods, 6, 92 (2017). https://doi.org/10.3390/foods6100092

L. Frémont, Life Sci. 66, 663 (2000). https://doi.org/10.1016/S0024-3205(99)00410-5

Y. Zhang, F. Liu, Y. Lin, L. Li, M. Chen, and L. Ni, J. Chem. 1, 4236525 (2022). https://doi.org/10.1155/2022/4236525

Rosheen, S. Sharma, and D. Utreja, ChemistrySelect, 8, e202204614 (2023). https://doi.org/10.1002/slct.202204614

B. Badhani, N. Sharmaa, and R. Kakkar, RSC Adv. 5, 27540 (2015). DOI https://doi.org/10.1039/C5RA01911G

Y. Yan, H. Tao, J. He, and S-Y. Huang, Nat. Protoc. 15, 1829 (2020). https://doi.org/10.1038/s41596-020-0312-x

S. Salentin, S. Schreiber, V. Haupt, M. Adasme, and M. Schroeder, Nucleic Acids Res. 43, W443 (2015). https://doi.org/10.1093/nar/gkv315

Published
2025-06-09
Cited
How to Cite
Malovytsia, U., Trusova, V., Thomsen, M., Vus, K., Zhyntniakivska, O., & Gorbenko, G. (2025). Polyphenol Interactions with Functional Proteins: A Molecular Docking Study. East European Journal of Physics, (2), 418-423. https://doi.org/10.26565/2312-4334-2025-2-51
Issue
No. 2 (2025): East European Journal of Physics
Section
Original Papers

Copyright (c) 2025 U. Malovytsia, V. Trusova, M. Thomsen, K. Vus, O. Zhyntniakivska, G. Gorbenko

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