Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications
Apstrakt
The interaction between phycocyanobilin (PCB), a bioactive
chromophore of blue-green cyanobacteria Spirulina’s phycobiliproteins,
and human alpha-2-macroglobulin (a2M), a universal
anti-proteinase, was investigated in this study under simulated
physiological conditions using spectroscopic techniques and a2M
activity assay. Protein a2M was found to bind PCB with a moderate
affinity, as assessed by spectrofluorimetric titration. The
binding constant was calculated to be 6.39105 M
1 at 25°C. The
binding of PCB to a2M did not cause significant change in the
secondary structure of the protein, as determined by circular
dichroism. PCB protected a2M from oxidative damage in the
presence of AAPH-induced free radical overproduction. PCB
binding also effectively preserved a2M anti-proteinase activity.
Since a2M is involved in controlling the action of enzymes during
the inflammatory process, the protection that PCB expresses
could indirectly influence the intensity and direction... of the body
response to impaired homeostasis, especially under oxidative
stress.
Ključne reči:
phycocyanobilin / interactionIzvor:
FEBS Open Bio, 2022, 12, Supplement 1, 304-304Izdavač:
- Wiley
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 - 200019 (Univerzitet u Beogradu, Institut za primenu nuklearne energije - INEP) (RS-MESTD-inst-2020-200019)
Napomena:
- The Biochemistry Global Summit, 25th IUBMB Congress, 46th FEBS Congress, 15th PABMB Congress, July 9-14, 2022, Lisbon, Portugal
Institucija/grupa
IHTMTY - CONF AU - Gligorijević, Nikola AU - Šunderić, Miloš AU - Minić, Simeon AU - Nedić, Olgica AU - Nikolić, Milan PY - 2022 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6822 AB - The interaction between phycocyanobilin (PCB), a bioactive chromophore of blue-green cyanobacteria Spirulina’s phycobiliproteins, and human alpha-2-macroglobulin (a2M), a universal anti-proteinase, was investigated in this study under simulated physiological conditions using spectroscopic techniques and a2M activity assay. Protein a2M was found to bind PCB with a moderate affinity, as assessed by spectrofluorimetric titration. The binding constant was calculated to be 6.39105 M 1 at 25°C. The binding of PCB to a2M did not cause significant change in the secondary structure of the protein, as determined by circular dichroism. PCB protected a2M from oxidative damage in the presence of AAPH-induced free radical overproduction. PCB binding also effectively preserved a2M anti-proteinase activity. Since a2M is involved in controlling the action of enzymes during the inflammatory process, the protection that PCB expresses could indirectly influence the intensity and direction of the body response to impaired homeostasis, especially under oxidative stress. PB - Wiley C3 - FEBS Open Bio T1 - Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications VL - 12 IS - Supplement 1 SP - 304 EP - 304 DO - 10.1002/2211-5463.13440 ER -
@conference{ author = "Gligorijević, Nikola and Šunderić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan", year = "2022", abstract = "The interaction between phycocyanobilin (PCB), a bioactive chromophore of blue-green cyanobacteria Spirulina’s phycobiliproteins, and human alpha-2-macroglobulin (a2M), a universal anti-proteinase, was investigated in this study under simulated physiological conditions using spectroscopic techniques and a2M activity assay. Protein a2M was found to bind PCB with a moderate affinity, as assessed by spectrofluorimetric titration. The binding constant was calculated to be 6.39105 M 1 at 25°C. The binding of PCB to a2M did not cause significant change in the secondary structure of the protein, as determined by circular dichroism. PCB protected a2M from oxidative damage in the presence of AAPH-induced free radical overproduction. PCB binding also effectively preserved a2M anti-proteinase activity. Since a2M is involved in controlling the action of enzymes during the inflammatory process, the protection that PCB expresses could indirectly influence the intensity and direction of the body response to impaired homeostasis, especially under oxidative stress.", publisher = "Wiley", journal = "FEBS Open Bio", title = "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications", volume = "12", number = "Supplement 1", pages = "304-304", doi = "10.1002/2211-5463.13440" }
Gligorijević, N., Šunderić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2022). Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in FEBS Open Bio Wiley., 12(Supplement 1), 304-304. https://doi.org/10.1002/2211-5463.13440
Gligorijević N, Šunderić M, Minić S, Nedić O, Nikolić M. Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications. in FEBS Open Bio. 2022;12(Supplement 1):304-304. doi:10.1002/2211-5463.13440 .
Gligorijević, Nikola, Šunderić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Interaction between alpha-2-macroglobulin and phycocyanobilin – structural and physiological implications" in FEBS Open Bio, 12, no. Supplement 1 (2022):304-304, https://doi.org/10.1002/2211-5463.13440 . .