TY  - JOUR
AU  - Zelenović, Nevena D.
AU  - Kojadinović, Milica I.
AU  - Filipović, Lidija
AU  - Vučić, Vesna M.
AU  - Milčić, Miloš K.
AU  - Arsic, Aleksndra
AU  - Popović, Milica M.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6257
AB  - Backgound/ObjectivesUrolithins (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.MethodsA 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.ResultsThe 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.ConclusionThe 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
DO  - 10.1177/1934578X231169366
ER  - 

@article{
author = "Zelenović, Nevena D. and Kojadinović, Milica I. and Filipović, Lidija and Vučić, Vesna M. and Milčić, Miloš K. and Arsic, Aleksndra and Popović, Milica M.",
year = "2023",
abstract = "Backgound/ObjectivesUrolithins (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.MethodsA 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.ResultsThe 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.ConclusionThe 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",
doi = "10.1177/1934578X231169366"
}

Zelenović, N. D., Kojadinović, M. I., Filipović, L., Vučić, V. M., Milčić, M. K., Arsic, A.,& Popović, M. M.. (2023). Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications
SAGE Publications., 18(5).
https://doi.org/10.1177/1934578X231169366

Zelenović ND, Kojadinović MI, Filipović L, Vučić VM, Milčić MK, Arsic A, Popović MM. Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications. 2023;18(5).
doi:10.1177/1934578X231169366 .

Zelenović, Nevena D., Kojadinović, Milica I., Filipović, Lidija, Vučić, Vesna M., Milčić, Miloš K., Arsic, Aleksndra, Popović, Milica M., "Interactions of Different Urolithins With Bovine Serum Albumin" in Natural Product Communications, 18, no. 5 (2023),
https://doi.org/10.1177/1934578X231169366 . .