Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress
Samo za registrovane korisnike
2023
Autori
Šunderić, Miloš![](/themes/MirageCER/images/orcid.png)
Gligorijević, Nikola
![](/themes/MirageCER/images/orcid.png)
Milčić, Miloš
![](/themes/MirageCER/images/orcid.png)
Minić, Simeon
![](/themes/MirageCER/images/orcid.png)
Nedić, Olgica
![](/themes/MirageCER/images/orcid.png)
Nikolić, Milan
![](/themes/MirageCER/images/orcid.png)
Članak u časopisu (Objavljena verzija)
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Informa UK Limited
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from ...oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.
Ključne reči:
Alpha-2-macroglobulin / phycocyanobilin / protein-ligand interactions / docking / spectroscopyIzvor:
Journal of Biomolecular Structure and Dynamics, 2023Izdavač:
- Taylor & Francis Group
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200026 (Univerzitet u Beogradu, Institut za hemiju, tehnologiju i metalurgiju - IHTM) (RS-MESTD-inst-2020-200026)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200019 (Univerzitet u Beogradu, Institut za primenu nuklearne energije - INEP) (RS-MESTD-inst-2020-200019)
Institucija/grupa
IHTMTY - JOUR AU - Šunderić, Miloš AU - Gligorijević, Nikola AU - Milčić, Miloš AU - Minić, Simeon AU - Nedić, Olgica AU - Nikolić, Milan PY - 2023 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6471 AB - Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process. PB - Taylor & Francis Group T2 - Journal of Biomolecular Structure and Dynamics T1 - Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress DO - 10.1080/07391102.2023.2248273 ER -
@article{ author = "Šunderić, Miloš and Gligorijević, Nikola and Milčić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan", year = "2023", abstract = "Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.", publisher = "Taylor & Francis Group", journal = "Journal of Biomolecular Structure and Dynamics", title = "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress", doi = "10.1080/07391102.2023.2248273" }
Šunderić, M., Gligorijević, N., Milčić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2023). Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics Taylor & Francis Group.. https://doi.org/10.1080/07391102.2023.2248273
Šunderić M, Gligorijević N, Milčić M, Minić S, Nedić O, Nikolić M. Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics. 2023;. doi:10.1080/07391102.2023.2248273 .
Šunderić, Miloš, Gligorijević, Nikola, Milčić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress" in Journal of Biomolecular Structure and Dynamics (2023), https://doi.org/10.1080/07391102.2023.2248273 . .