Naslov (eng)

Ligand binding to fibrinogen influences its structure and function

Autor

Gligorijević, Nikola
Nedić, Olgica
Ćirković Veličković, Tanja
Nikolić, Milan
Lević, Steva
Radomirović, Mirjana
Minić, Simeon

Opis (eng)

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.

Jezik

engleski

Datum

2021

Licenca

Ovo delo je licencirano pod uslovima licence
Creative Commons CC BY 4.0 - Creative Commons Autorstvo 4.0 International License.

http://creativecommons.org/licenses/by/4.0/legalcode

Predmet

bilirubin, dihydrolipoic acid, fibrinogen, protein function, protein-ligand interaction, protein structure, resveratrol

Deo kolekcije (1)

o:25140

Radovi Instituta za primenu nuklearne energije - INEP