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Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation

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2020
j.ijbiomac.2020_acc.pdf (5.492Mb)
Authors
Gligorijević, Nikola
Šukalović, Vladimir
Penezić, Ana
Nedić, Olgica
Article (Accepted Version)
,
Elsevier
Metadata
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Abstract
A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation p...rocess, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.

Keywords:
Protein interaction / Molecular modelling / Protein function
Source:
International Journal of Biological Macromolecules, 2020, 147, 319-325
Publisher:
  • Elsevier
Funding / projects:
  • Structural characterisation of the insulin-like growth factor (IGF) binding proteins and IGF receptors, their interactions with other physiological molecules and alterations in metabolic disorders (RS-173042)
Note:
  • This is the peer-reviewed version of the article: International Journal of Biological Macromolecules, 2020, 147, 319-325, doi: https://dx.doi.org/10.1016/j.ijbiomac.2020.01.098
  • The published version: http://cer.ihtm.bg.ac.rs/handle/123456789/3378

DOI: 10.1016/j.ijbiomac.2020.01.098

ISSN: 0141-8130

WoS: 000525864700036

Scopus: 2-s2.0-85077757227
[ Google Scholar ]
6
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URI
https://cer.ihtm.bg.ac.rs/handle/123456789/3385
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Penezić, Ana
AU  - Nedić, Olgica
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3385
AB  - A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation
VL  - 147
SP  - 319
EP  - 325
DO  - 10.1016/j.ijbiomac.2020.01.098
ER  - 
@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Penezić, Ana and Nedić, Olgica",
year = "2020",
abstract = "A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation",
volume = "147",
pages = "319-325",
doi = "10.1016/j.ijbiomac.2020.01.098"
}
Gligorijević, N., Šukalović, V., Penezić, A.,& Nedić, O.. (2020). Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules
Elsevier., 147, 319-325.
https://doi.org/10.1016/j.ijbiomac.2020.01.098
Gligorijević N, Šukalović V, Penezić A, Nedić O. Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules. 2020;147:319-325.
doi:10.1016/j.ijbiomac.2020.01.098 .
Gligorijević, Nikola, Šukalović, Vladimir, Penezić, Ana, Nedić, Olgica, "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation" in International Journal of Biological Macromolecules, 147 (2020):319-325,
https://doi.org/10.1016/j.ijbiomac.2020.01.098 . .

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