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Molecular Interaction of Fibrinogen With Zeolite Nanoparticles Publisher Pubmed



Derakhshankhah H1, 2 ; Hosseini A3 ; Taghavi F4 ; Jafari S2 ; Lotfabadi A1, 2, 4 ; Ejtehadi MR5, 6 ; Shahbazi S7 ; Fattahi A2 ; Ghasemi A4 ; Barzegari E2 ; Evini M4 ; Saboury AA4 ; Shahri SMK8 ; Ghaemi B9 Show All Authors
Authors
  1. Derakhshankhah H1, 2
  2. Hosseini A3
  3. Taghavi F4
  4. Jafari S2
  5. Lotfabadi A1, 2, 4
  6. Ejtehadi MR5, 6
  7. Shahbazi S7
  8. Fattahi A2
  9. Ghasemi A4
  10. Barzegari E2
  11. Evini M4
  12. Saboury AA4
  13. Shahri SMK8
  14. Ghaemi B9
  15. Ng EP10
  16. Awala H11
  17. Omrani F12
  18. Nabipour I12
  19. Raoufi M13
  20. Dinarvand R13
  21. Shahpasand K14
  22. Mintova S11
  23. Hajipour MJ12, 15
  24. Mahmoudi M16
Show Affiliations
Authors Affiliations
  1. 1. Nano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
  2. 2. Pharmacutical Sciences Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
  3. 3. Institute for Nanoscience and Nanotechnology and Center of Excellence in Complex Systems and Condensed Matter (CSCM), Sharif University of Technology, Tehran, 1458889694, Iran
  4. 4. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  5. 5. Department of Physics, Sharif University of Technology, P. O. Box 11155-9161, Tehran, Iran
  6. 6. Center of Excellence in Complex Systems and Condensed Matter (CSCM), Sharif University of Technology, Tehran, 1458889694, Iran
  7. 7. School of Biology College of Science, University of Tehran, Tehran, Iran
  8. 8. Department of Chemical Engineering, Pennsylvania State University, University Park, 16802, PA, United States
  9. 9. Department of Medical Nanotechnology, School of Advanced Technologies in Medicine (SATiM), Tehran University of Medical Sciences, Tehran, 1417755469, Iran
  10. 10. School of Chemical Sciences, Universiti Sains Malaysia, Gelugor, 11800 USM, Malaysia
  11. 11. Laboratory of Catalysis and Spectroscopy, ENSICAEN, University of Caen, CNRS, 6 Boulevard du Marechal Juin, Caen, 14050, France
  12. 12. Persian Gulf Marine Biotechnology Research Center, the Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Bushehr, 75147, Iran
  13. 13. Nanotechnology Research Center, Faculty of Pharmacy, Department of Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  14. 14. Department of Brain and Cognitive Sciences, Cell Science Research Center, Royan Institute for Stem Cell Biology and Technology, ACECR, Tehran, Iran
  15. 15. Non-Communicable Diseases Research Center, Endocrinology and Metabolism Population Sciences Institute, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  16. 16. Department of Anesthesiology, Brigham and Women’s Hospital, Harvard Medical School, Boston, 02115, MA, United States

Source: Scientific Reports Published:2019


Abstract

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. © 2019, The Author(s).
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