Molecular interaction of fibrinogen with zeolite nanoparticles

Hossein Derakhshankhah (1) , Atiyeh Hosseini (2) , Fereshteh Taghavi (3) , Samira Jafari (1) , Alireza Lotfabadi (1) , Mohammad Reza Ejtehadi (2) , Sahba Shahbazi (3) , Ali Fattahi (1) , Atiyeh Ghasemi (3) , Ebrahim Barzegari (1) , Mina Evini (3) , Ali Akbar Saboury , Seyed Mehdi Kamali Shahri (4) , Behnaz Ghaemi (5) , Eng-Poh Ng (6) , Hussein Awala (7) , Fatemeh Omrani (8) , Iraj Nabipour (8) , Mohammad Raoufi (5) , Rassoul Dinarvand (5) , Koorosh Shahpasand (9) , Svetlana Mintova (7) , Mohammad Javad Hajipour (10) , Morteza Mahmoudi (11)

1 Kermanshah University of Medical Sciences
2 SUT - Sharif University of Technology [Tehran]
3 University of Tehran
4 Penn State - Pennsylvania State University
5 TUMS - Tehran University of Medical Sciences
6 USM - Universiti Sains Malaysia
7 LCS - Laboratoire catalyse et spectrochimie
8 Bushehr University of Medical Sciences
9 ACECR - Academic Center for Education, Culture and Research
10 Persian Gulf Marine Biotechnology Research Center
11 HMS - Harvard Medical School [Boston]

Fibrinogen is one of the key proteins that participate in the protein corona composition of many types of nanoparticles (NPs), and its conformational changes are crucial for activation of immune systems. Recently, we demonstrated that the fibrinogen highly contributed in the protein corona composition at the surface of zeolite nanoparticles. Therefore, understanding the interaction of fibrinogen with zeolite nanoparticles in more details could shed light of their safe applications in medicine. Thus, we probed the molecular interactions between fibrinogen and zeolite nanoparticles using both experimental and simulation approaches. The results indicated that fibrinogen has a strong and thermodynamically favorable interaction with zeolite nanoparticles in a non-cooperative manner. Additionally, fibrinogen experienced a substantial conformational change in the presence of zeolite nanoparticles through a concentration-dependent manner. Simulation results showed that both E- and D-domain of fibrinogen are bound to the EMT zeolite NPs via strong electrostatic interactions, and undergo structural changes leading to exposing normally buried sequences. D-domain has more contribution in this interaction and the C-terminus of γ chain (γ377–394), located in D-domain, showed the highest level of exposure compared to other sequences/residues.

Mots clés: Zeolite nanoparticles; Fibrinogen; Conformational change; Protein-nanoparticles interactions

Domaines: Biophysique

Hossein Derakhshankhah, Atiyeh Hosseini, Fereshteh Taghavi, Samira Jafari, Alireza Lotfabadi, et al.. Molecular interaction of fibrinogen with zeolite nanoparticles. Scientific Reports, 2019, 9 (1), pp.1558. ⟨10.1038/s41598-018-37621-4⟩. ⟨hal-02047597⟩