Ligand binding to fibrinogen influences its structure and function
Authors
Gligorijević, NikolaMinić, Simeon L.
Radomirović, Mirjana Ž.
Lević, Steva M.
Nikolić, Milan
Ćirković-Veličković, Tanja
Nedić, Olgica
Article (Published version)
Metadata
Show full item recordAbstract
Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.
Keywords:
bilirubin / dihydrolipoic acid / fibrinogen / protein function / protein-ligand interaction / protein structure / resveratrolSource:
Biologia Serbica, 2021, 43, 1Publisher:
- University of Novi Sad - Faculty of Sciences, Department of Biology
Funding / projects:
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200168 (University of Belgrade, Faculty of Chemistry) (RS-MESTD-inst-2020-200168)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200019 (University of Belgrade, Institute for the Application of Nuclear Energy - INEP) (RS-MESTD-inst-2020-200019)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200116 (University of Belgrade, Faculty of Agriculture) (RS-MESTD-inst-2020-200116)
- Belgian Special Research Fund BOF STG, grant number 01N01718.
- Serbian Academy of Sciences and Arts, grant number F-26.
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-H2020-810752)
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Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Gligorijević, Nikola AU - Minić, Simeon L. AU - Radomirović, Mirjana Ž. AU - Lević, Steva M. AU - Nikolić, Milan AU - Ćirković-Veličković, Tanja AU - Nedić, Olgica PY - 2021 UR - http://cherry.chem.bg.ac.rs/handle/123456789/4862 AB - Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text. PB - University of Novi Sad - Faculty of Sciences, Department of Biology T2 - Biologia Serbica T1 - Ligand binding to fibrinogen influences its structure and function VL - 43 IS - 1 DO - 10.5281/zenodo.5512285 ER -
@article{ author = "Gligorijević, Nikola and Minić, Simeon L. and Radomirović, Mirjana Ž. and Lević, Steva M. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica", year = "2021", abstract = "Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.", publisher = "University of Novi Sad - Faculty of Sciences, Department of Biology", journal = "Biologia Serbica", title = "Ligand binding to fibrinogen influences its structure and function", volume = "43", number = "1", doi = "10.5281/zenodo.5512285" }
Gligorijević, N., Minić, S. L., Radomirović, M. Ž., Lević, S. M., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica University of Novi Sad - Faculty of Sciences, Department of Biology., 43(1). https://doi.org/10.5281/zenodo.5512285
Gligorijević N, Minić SL, Radomirović MŽ, Lević SM, Nikolić M, Ćirković-Veličković T, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica. 2021;43(1). doi:10.5281/zenodo.5512285 .
Gligorijević, Nikola, Minić, Simeon L., Radomirović, Mirjana Ž., Lević, Steva M., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Biologia Serbica, 43, no. 1 (2021), https://doi.org/10.5281/zenodo.5512285 . .