Affiliations 

  • 1 Nano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
  • 2 Institute for Nanoscience and Nanotechnology and Center of Excellence in Complex Systems and Condensed Matter (CSCM), Sharif University of Technology, Tehran, 1458889694, Iran
  • 3 Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  • 4 Pharmacutical Sciences Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
  • 5 Department of Physics, Sharif University of Technology, P. O. Box 11155-9161, Tehran, Iran
  • 6 School of Biology College of Science, University of Tehran, Tehran, Iran
  • 7 Department of Chemical Engineering, Pennsylvania State University, University Park, PA, 16802, United States
  • 8 Department of Medical Nanotechnology, School of Advanced Technologies in Medicine (SATiM), Tehran University of Medical Sciences, Tehran, 1417755469, Iran
  • 9 School of Chemical Sciences, Universiti Sains Malaysia, Gelugor, 11800 USM, Malaysia
  • 10 Laboratory of Catalysis and Spectroscopy, ENSICAEN, University of Caen, CNRS, 6 Boulevard du Marechal Juin, 14050, Caen, France
  • 11 Persian Gulf Marine Biotechnology Research Center, the Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Bushehr, 75147, Iran
  • 12 Nanotechnology Research Center, Faculty of Pharmacy, Department of Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  • 13 Department of Brain and Cognitive Sciences, Cell Science Research Center, Royan Institute for Stem Cell Biology and Technology, ACECR, Tehran, Iran
  • 14 Laboratory of Catalysis and Spectroscopy, ENSICAEN, University of Caen, CNRS, 6 Boulevard du Marechal Juin, 14050, Caen, France. mintova@ensicaen.fr
  • 15 Persian Gulf Marine Biotechnology Research Center, the Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Bushehr, 75147, Iran. mj.hajipour@ncdrc.info
  • 16 Department of Anesthesiology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, 02115, United States. mmahmoudi@bwh.harvard.edu
Sci Rep, 2019 02 07;9(1):1558.
PMID: 30733474 DOI: 10.1038/s41598-018-37621-4

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 (γ377-394), located in D-domain, showed the highest level of exposure compared to other sequences/residues.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.