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Ligand binding to fibrinogen influences its structure and function

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2021
Ligand_binding_to_pub_2021.pdf (4.067Mb)
Authors
Gligorijević, Nikola
Minić, Simeon L.
Radomirović, Mirjana Ž.
Lević, Steva M.
Nikolić, Milan
Ćirković-Veličković, Tanja
Nedić, Olgica
Article (Published version)
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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.
Keywords:
bilirubin / dihydrolipoic acid / fibrinogen / protein function / protein-ligand interaction / protein structure / resveratrol
Source:
Biologia Serbica, 2021, 43, 1
Publisher:
  • University of Novi Sad - Faculty of Sciences, Department of Biology
Funding / projects:
  • Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200168 (University of Belgrade, Faculty of Chemistry) (RS-200168)
  • Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200019 (University of Belgrade, Institute for the Application of Nuclear Energy - INEP) (RS-200019)
  • Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200116 (University of Belgrade, Faculty of Agriculture) (RS-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-810752)

DOI: 10.5281/zenodo.5512285

ISSN: 2217-766X

[ Google Scholar ]
URI
http://cherry.chem.bg.ac.rs/handle/123456789/4862
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - 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 . .

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