Interactions of Different Urolithins With Bovine Serum Albumin
Аутори
Zelenović, NevenaKojadinovic, Milica
Filipović, Lidija
Vucic, Vesna
Milčić, Miloš
Arsić, Aleksndra
Popović, Milica
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenchi...ng the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236 ± 5706 and 69653 ± 14922, respectively, while for UROAG and UROBG, these values were 15179 ± 2770 and 9462 ± 1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.
Кључне речи:
fluorescence quenching / bovine serum albumin / ellagitannins / elagic acid / molecular docking / urolithinИзвор:
Natural Product Communications, 2023, 18, 5, 1934578X2311693-Издавач:
- SAGE Publications
Финансирање / пројекти:
- info:eu-repo/grantAgreement/MESTD/inst-2020/200288/RS//istarstvo Prosvete, Nauke i Tehnološkog Razvoja https://doi.org/10.13039/501100004564 : 451-03-9/2021-14/200288 (RS-MESTD-inst-2020-200288)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200015 (Универзитет у Београду, Институт за медицинска истраживања) (RS-MESTD-inst-2020-200015)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200026 (Универзитет у Београду, Институт за хемију, технологију и металургију - ИХТМ) (RS-MESTD-inst-2020-200026)
DOI: 10.1177/1934578X231169366
ISSN: 1934-578X; 1555-9475
Scopus: 2-s2.0-85158914449
Институција/група
IHTMTY - JOUR AU - Zelenović, Nevena AU - Kojadinovic, Milica AU - Filipović, Lidija AU - Vucic, Vesna AU - Milčić, Miloš AU - Arsić, Aleksndra AU - Popović, Milica PY - 2023 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/7223 AB - Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236 ± 5706 and 69653 ± 14922, respectively, while for UROAG and UROBG, these values were 15179 ± 2770 and 9462 ± 1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood. PB - SAGE Publications T2 - Natural Product Communications T1 - Interactions of Different Urolithins With Bovine Serum Albumin VL - 18 IS - 5 SP - 1934578X2311693 DO - 10.1177/1934578X231169366 ER -
@article{ author = "Zelenović, Nevena and Kojadinovic, Milica and Filipović, Lidija and Vucic, Vesna and Milčić, Miloš and Arsić, Aleksndra and Popović, Milica", year = "2023", abstract = "Backgound/Objectives Urolithins (UROs) are the metabolites derived from the gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in the intestine, UROs are transported through the systemic circulation to various tissues where they can express their biological function as antimicrobial, anti-inflammatory, and anticancer agents. In addition to blood plasma, where they can be found as glucuronide and sulfate conjugates, they are also found in urine. Therefore, the interactions of UROs with serum proteins are of great clinical interest. Methods A powerful technique for examining these urolithin-serum protein interactions is fluorescence spectroscopy. Bovine serum albumin (BSA) is a particularly suitable model protein because it is readily available, affordable, and similar to human serum albumin. This work aimed to study the binding of UROs (urolithin A, UROA and urolithin B, UROB) and their glucuronide conjugates (UROAG and UROBG) to BSA by quenching the intrinsic fluorescence of protein. Results The spectra obtained showed that the binding process is influenced by the polyphenol's structure and the conjugation process with the glucuronide. The calculated Stern Vollmer binding constants (Ksv): UROA and UROB Ksv were 59236 ± 5706 and 69653 ± 14922, respectively, while for UROAG and UROBG, these values were 15179 ± 2770 and 9462 ± 1955, respectively, which showed that the binding affinity decreased with glucuronidation. Molecular docking studies confirmed that all of the studied molecules will bind favorably to BSA. The preferential binding site for both UROs and UROGs is Sudlow I, while UROs will also bind to Sudlow II. URO-Gs can bind to BSA in the cleft region with lower binding scores than for the Sudlow I binding site. Conclusion The aglycone's higher hydrophobicity increases the binding affinity to BSA, thus reducing its bioavailability in the blood.", publisher = "SAGE Publications", journal = "Natural Product Communications", title = "Interactions of Different Urolithins With Bovine Serum Albumin", volume = "18", number = "5", pages = "1934578X2311693", doi = "10.1177/1934578X231169366" }
Zelenović, N., Kojadinovic, M., Filipović, L., Vucic, V., Milčić, M., Arsić, A.,& Popović, M.. (2023). Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications SAGE Publications., 18(5), 1934578X2311693. https://doi.org/10.1177/1934578X231169366
Zelenović N, Kojadinovic M, Filipović L, Vucic V, Milčić M, Arsić A, Popović M. Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications. 2023;18(5):1934578X2311693. doi:10.1177/1934578X231169366 .
Zelenović, Nevena, Kojadinovic, Milica, Filipović, Lidija, Vucic, Vesna, Milčić, Miloš, Arsić, Aleksndra, Popović, Milica, "Interactions of Different Urolithins With Bovine Serum Albumin" in Natural Product Communications, 18, no. 5 (2023):1934578X2311693, https://doi.org/10.1177/1934578X231169366 . .