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Probing Fibronectin Conformation on a Protein Corona Layer Around Nanoparticles Publisher Pubmed



Raoufi M1, 2 ; Hajipour MJ3, 4 ; Kamali Shahri SM5 ; Schoen I6 ; Linn U7 ; Mahmoudi M8
Authors
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Authors Affiliations
  1. 1. Nanotechnology Research Centre, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 1417614411, Iran
  2. 2. Department of New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Heisenbergstraße 3, Stuttgart, D-70569, Germany
  3. 3. Persian Gulf Marine Biotechnology Research Center, Persian Gulf Biomedical Sciences Research Institute, Bushehr University of Medical Sciences, Bushehr, 75147, 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. Department of Chemical Engineering, Pennsylvania State University, University Park, 16802, PA, United States
  6. 6. Laboratory of Applied Mechanobiology, Department of Health Sciences and Technology, ETH Zurich, Vladimir-Prelog Weg 4, Zurich, CH-8093, Switzerland
  7. 7. Fachbereich Physik/Chemie, Philipps-Universitat Marburg, Marburg, Germany
  8. 8. Center for Nanomedicine, Department of Anesthesiology, Brigham and Women's Hospital, Harvard Medical School, Boston, 02115, MA, United States

Source: Nanoscale Published:2018


Abstract

Protein unfolding induced by nanoparticles (NPs) can lead to exposure of cryptic epitopes that might dictate biological identity and affect NP biological fate (e.g., blood circulation time, biodistribution, and tumor accumulation). Here, we monitor the conformation of fluorescence resonance energy transfer (FRET)-labelled fibronectin (FN) on corona-coated gold NPs. We found that the labelled FN proteins, which directly accessed the gold NP surface, underwent more pronounced conformational changes than those associated with the protein corona via protein-protein interactions. FRET and liquid chromatography-mass spectrometry analyses demonstrated that NP size/concentration, pH change, and the level of surface coverage by the corona can tune the accessibility of labelled FN to the gold NP surface. Although some subsequently adsorbing proteins accessed the NP surface thanks to incomplete surface coverage and protein exchange (the Vroman effect), most outer-layer proteins could not directly bind to the NP surface, blocked by pre-adsorbed corona layers. This finding was also partially confirmed by isothermal titration calorimetry (ITC) analysis. These results suggest the proof-of-concept that outermost-layer proteins with modestly changed conformation rather than unfolded proteins at the gold NP surface effectively create the NPs' biological identity, which might have important implications on biological fates of gold NPs. © 2018 The Royal Society of Chemistry.