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Zeolite Nanoparticles Inhibit Aβ-Fibrinogen Interaction and Formation of a Consequent Abnormal Structural Clot Publisher Pubmed



Derakhshankhah H1, 2, 3 ; Hajipour MJ1, 3, 4, 5 ; Barzegari E6 ; Lotfabadi A1, 2, 3 ; Ferdousi M7 ; Saboury AA6 ; Ng EP8 ; Raoufi M2 ; Awala H9 ; Mintova S9 ; Dinarvand R2, 3 ; Mahmoudi M2, 3, 10
Authors
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Authors Affiliations
  1. 1. Department of Pharmaceutical Biomaterials, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  2. 2. Nanotechnology Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  3. 3. Department of Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  4. 4. Non-Communicable Diseases Research Center, Endocrinology and Metabolism Population Sciences Institute, Tehran University of Medical Sciences, Tehran, 13169-43551, Iran
  5. 5. Persian Gulf Marine Biotechnology Research Center, Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Bushehr, 75147, Iran
  6. 6. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  7. 7. School of Biology College of Science, University of Tehran, Tehran, Iran
  8. 8. School of Chemical Sciences, Universiti Sains Malaysia, USM, 11800, Malaysia
  9. 9. Laboratory of Catalysis and Spectroscopy, ENSICAEN, University of Caen, CNRS, 6 Boulevard du Marechal Juin, Caen, 14050, France
  10. 10. Department of Anesthesiology, Brigham and Women's Hospital, Harvard Medical School, Boston, 02115, MA, United States

Source: ACS Applied Materials and Interfaces Published:2016


Abstract

EMT-type zeolite nanoparticles (EMT NPs) with particle size of 10-20 nm and external surface area of 200 m2/g have shown high selective affinity toward plasma protein (fibrinogen). Besides, the EMT NPs have demonstrated no adverse effect on blood coagulation hemostasis. Therefore, it was envisioned that the EMT NPs could inhibit possible β-amyloid (Aβ)-fibrinogen interactions that result in the formation of structurally abnormal clots, which are resistant to lysis, in cerebral vessels of patients with Alzheimer disease (AD). To evaluate this hypothesis, the clot formation and degradation of Aβ-fibrinogen in the presence and absence of the EMT zeolite NPs were assessed. The results clearly showed that the delay in clot dissolution was significantly reduced in the presence of zeolite NPs. By formation of protein corona, the EMT NPs showed a negligible reduction in their inhibitory strength. Docking of small molecules (Aβ-fibrinogen) introduced a novel potential inhibitory candidate. The zeolite NPs showed similar inhibitory effects on binding of fibrinogen to both Aβ(25-35) and/or Aβ(1-42). This indicates that the inhibitory strength of these NPs is independent of Aβ sequence, and it is suggested that the zeolite NPs adsorb fibrinogen and specifically obstruct their Aβ binding sites. Therefore, the zeolite NPs can be the safe and effective inhibitors in preventing Aβ-fibrinogen interaction and consequent cognitive damage. © 2016 American Chemical Society.
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