Characterisation and the effects of bilirubin binding to human fibrinogen
Аутори
Gligorijević, NikolaMinić, Simeon L.
Robajac, Dragana B.
Nikolić, Milan
Ćirković-Veličković, Tanja
Nedić, Olgica
Чланак у часопису (Рецензирана верзија)
Метаподаци
Приказ свих података о документуАпстракт
Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventin...g its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
Кључне речи:
Binding / Circular dichroism / Coagulation / Fluorimetry / Protein oxidationИзвор:
International Journal of Biological Macromolecules, 2019, 128, 74-79Финансирање / пројекти:
- Структурне карактеристике везујућих протеина и рецептора за инсулину сличне факторе раста (IGF), њихове интеракције са другим физиолошким молекулима и промене код поремећаја метаболизма (RS-MESTD-Basic Research (BR or ON)-173042)
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-172024)
Напомена:
- This is the peer-reviewed version of the following article: Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica, 2019. Characterisation and the effects of bilirubin binding to human fibrinogen. International Journal of Biological Macromolecules. 128, 74-79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/2937
DOI: 10.1016/j.ijbiomac.2019.01.124
ISSN: 0141-8130
WoS: 000463305100010
Scopus: 2-s2.0-85060455696
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Gligorijević, Nikola AU - Minić, Simeon L. AU - Robajac, Dragana B. AU - Nikolić, Milan AU - Ćirković-Veličković, Tanja AU - Nedić, Olgica PY - 2019 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2825 AB - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction. T2 - International Journal of Biological Macromolecules T1 - Characterisation and the effects of bilirubin binding to human fibrinogen VL - 128 SP - 74 EP - 79 DO - 10.1016/j.ijbiomac.2019.01.124 ER -
@article{ author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica", year = "2019", abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.", journal = "International Journal of Biological Macromolecules", title = "Characterisation and the effects of bilirubin binding to human fibrinogen", volume = "128", pages = "74-79", doi = "10.1016/j.ijbiomac.2019.01.124" }
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules, 128, 74-79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules. 2019;128:74-79. doi:10.1016/j.ijbiomac.2019.01.124 .
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" in International Journal of Biological Macromolecules, 128 (2019):74-79, https://doi.org/10.1016/j.ijbiomac.2019.01.124 . .