TY  - JOUR
AU  - Zelenović, Nevena
AU  - Kojadinović, Milica
AU  - Filipović, Lidija
AU  - Vučić, Vesna
AU  - Milčić, Miloš
AU  - Arsić, Aleksandra
AU  - Popović, Milica
PY  - 2023
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1309
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
T2  - Natural Product Communications
T1  - Interactions of Different Urolithins With Bovine Serum Albumin
IS  - 5
VL  - 18
DO  - 10.1177/1934578X231169366
ER  - 

@article{
author = "Zelenović, Nevena and Kojadinović, Milica and Filipović, Lidija and Vučić, Vesna and Milčić, Miloš and Arsić, Aleksandra 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",
journal = "Natural Product Communications",
title = "Interactions of Different Urolithins With Bovine Serum Albumin",
number = "5",
volume = "18",
doi = "10.1177/1934578X231169366"
}

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

Zelenović N, Kojadinović M, Filipović L, Vučić V, Milčić M, Arsić A, Popović M. Interactions of Different Urolithins With Bovine Serum Albumin. in Natural Product Communications. 2023;18(5).
doi:10.1177/1934578X231169366 .

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

TY  - JOUR
AU  - Filipović, Lidija
AU  - Kojadinović, Milica
AU  - Popović, Milica
PY  - 2022
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1204
AB  - Exosomes are a sub-group of extracellular vesicles, playing an important part in a cell-cell communication in many physiological and pathological conditions. Their size and competence for transferring material to recipient cells make them a promising nanocarrier for clinical use. Their non-immunogenic nature, similar to the body's own structure make them far superior transporters compared to liposomes and polymeric nanoparticles. This review, will provide an overview of exosome biogenesis, biological role, and purification methods. The focus of this manuscript will be to summarize specific applications of exosomes and exosome-mimetics as drug delivery systems in pharmaceutical drug development. We will describe drug-loading approaches, in vivo and in vitro exosome tracing methods, specific modifications and examples of the delivery of therapeutic and imaging molecules from a variety of biological origins. Challenges in the translation of exosome-based drug carriers to clinical use will also be discussed in this review.
PB  - Elsevier
T2  - Journal of Drug Delivery Science and Technology
T1  - Exosomes and exosome-mimetics as targeted drug carriers: Where we stand and what the future holds?
SP  - 103057
VL  - 68
DO  - 10.1016/j.jddst.2021.103057
ER  - 

@article{
author = "Filipović, Lidija and Kojadinović, Milica and Popović, Milica",
year = "2022",
abstract = "Exosomes are a sub-group of extracellular vesicles, playing an important part in a cell-cell communication in many physiological and pathological conditions. Their size and competence for transferring material to recipient cells make them a promising nanocarrier for clinical use. Their non-immunogenic nature, similar to the body's own structure make them far superior transporters compared to liposomes and polymeric nanoparticles. This review, will provide an overview of exosome biogenesis, biological role, and purification methods. The focus of this manuscript will be to summarize specific applications of exosomes and exosome-mimetics as drug delivery systems in pharmaceutical drug development. We will describe drug-loading approaches, in vivo and in vitro exosome tracing methods, specific modifications and examples of the delivery of therapeutic and imaging molecules from a variety of biological origins. Challenges in the translation of exosome-based drug carriers to clinical use will also be discussed in this review.",
publisher = "Elsevier",
journal = "Journal of Drug Delivery Science and Technology",
title = "Exosomes and exosome-mimetics as targeted drug carriers: Where we stand and what the future holds?",
pages = "103057",
volume = "68",
doi = "10.1016/j.jddst.2021.103057"
}

Filipović, L., Kojadinović, M.,& Popović, M.. (2022). Exosomes and exosome-mimetics as targeted drug carriers: Where we stand and what the future holds?. in Journal of Drug Delivery Science and Technology
Elsevier., 68, 103057.
https://doi.org/10.1016/j.jddst.2021.103057

Filipović L, Kojadinović M, Popović M. Exosomes and exosome-mimetics as targeted drug carriers: Where we stand and what the future holds?. in Journal of Drug Delivery Science and Technology. 2022;68:103057.
doi:10.1016/j.jddst.2021.103057 .

Filipović, Lidija, Kojadinović, Milica, Popović, Milica, "Exosomes and exosome-mimetics as targeted drug carriers: Where we stand and what the future holds?" in Journal of Drug Delivery Science and Technology, 68 (2022):103057,
https://doi.org/10.1016/j.jddst.2021.103057 . .