TY  - JOUR
AU  - Zelenović, Nevena D.
AU  - Filipović, Lidija
AU  - Popović, Milica M.
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6356
AB  - Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.
PB  - Springer
T2  - Biochemistry (Moscow)
T1  - Recent Developments in Bioprocessing of Recombinant Antibody Fragments
VL  - 88
IS  - 9
SP  - 1191
EP  - 1204
DO  - 10.1134/S0006297923090018
ER  - 

@article{
author = "Zelenović, Nevena D. and Filipović, Lidija and Popović, Milica M.",
year = "2023",
abstract = "Biotechnological and biomedical applications of antibodies have been on a steady rise since the 1980s. As unique and highly specific bioreagents, monoclonal antibodies (mAbs) have been widely exploited and approved as therapeutic agents. However, the use of mAbs has limitations for therapeutic applications. Antibody fragments (AbFs) with preserved antigen-binding sites have a significant potential to overcome the disadvantages of conventional mAbs, such as heterogeneous tissue distribution after systemic administration, especially in solid tumors, and Fc-mediated bystander activation of the immune system. AbFs possess better biodistribution coefficient due to lower molecular weight. They preserve the functional features of mAbs, such as antigen specificity and binding, while at the same time, ensuring much better tissue penetration. An additional benefit of AbFs is the possibility of their production in bacterial and yeast cells due to the small size, more robust structure, and lack of posttranslational modifications. In this review, we described current approaches to the AbF production with recent examples of AbF synthesis in bacterial and yeast expression systems and methods for the production optimization.",
publisher = "Springer",
journal = "Biochemistry (Moscow)",
title = "Recent Developments in Bioprocessing of Recombinant Antibody Fragments",
volume = "88",
number = "9",
pages = "1191-1204",
doi = "10.1134/S0006297923090018"
}

Zelenović, N. D., Filipović, L.,& Popović, M. M.. (2023). Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow)
Springer., 88(9), 1191-1204.
https://doi.org/10.1134/S0006297923090018

Zelenović ND, Filipović L, Popović MM. Recent Developments in Bioprocessing of Recombinant Antibody Fragments. in Biochemistry (Moscow). 2023;88(9):1191-1204.
doi:10.1134/S0006297923090018 .

Zelenović, Nevena D., Filipović, Lidija, Popović, Milica M., "Recent Developments in Bioprocessing of Recombinant Antibody Fragments" in Biochemistry (Moscow), 88, no. 9 (2023):1191-1204,
https://doi.org/10.1134/S0006297923090018 . .

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 . .