TY - JOUR
T1 - Molecular interaction of fibrinogen with zeolite nanoparticles
AU - Derakhshankhah, Hossein
AU - Hosseini, Atiyeh
AU - Taghavi, Fereshteh
AU - Jafari, Samira
AU - Lotfabadi, Alireza
AU - Ejtehadi, Mohammad Reza
AU - Shahbazi, Sahba
AU - Fattahi, Ali
AU - Ghasemi, Atiyeh
AU - Barzegari, Ebrahim
AU - Evini, Mina
AU - Saboury, Ali Akbar
AU - Shahri, Seyed Mehdi Kamali
AU - Ghaemi, Behnaz
AU - Ng, Eng Poh
AU - Awala, Hussein
AU - Omrani, Fatemeh
AU - Nabipour, Iraj
AU - Raoufi, Mohammad
AU - Dinarvand, Rassoul
AU - shahpasand, Koorosh
AU - Mintova, Svetlana
AU - Hajipour, Mohammad Javad
AU - Mahmoudi, Morteza
N1 - Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - 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 (γ 377–394 ), located in D-domain, showed the highest level of exposure compared to other sequences/residues.
AB - 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 (γ 377–394 ), located in D-domain, showed the highest level of exposure compared to other sequences/residues.
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U2 - 10.1038/s41598-018-37621-4
DO - 10.1038/s41598-018-37621-4
M3 - Article
C2 - 30733474
AN - SCOPUS:85061293803
SN - 2045-2322
VL - 9
JO - Scientific reports
JF - Scientific reports
IS - 1
M1 - 1558
ER -