Biomolecular Corona Dictates Aβ Fibrillation Process Publisher Pubmed



Lotfabadi A^{1, 2, 3} ; Hajipour MJ^{4, 5} ; Derakhshankhah H⁶ ; Peirovi A⁷ ; Saffar S⁷ ; Shams E⁸ ; Fatemi E⁸ ; Barzegari E⁹ ; Sarvari S⁹ ; Moakedi F¹⁰ ; Ferdousi M¹¹ ; Atyabi F^{2, 3} ; Saboury AA⁹ ; Dinarvand R^{2, 3} Show Affiliations
Source: ACS Chemical Neuroscience Published:2018

Abstract

Amyloid beta (Aβ), which forms toxic oligomers and fibrils in brain tissues of patients with Alzheimer's disease, is broadly used as a model protein to probe the effect of nanoparticles (NPs) on oligomerization and fibrillation processes. However, the majority of the reports in the field have ignored the effect of the biomolecular corona on the fibrillogenesis of the Aβ proteins. The biomolecular corona, which is a layer composed of various types of biomolecules that covers the surface of NPs upon their interaction with biological fluids, determines the biological fates of NPs. Therefore, during in vivo interaction of NPs with Aβ protein, what the Aβ actually sees is the human plasma and/or cerebrospinal fluid (CSF) biomolecular-coated NPs rather than the pristine surface of NPs. Here, to mimic the in vivo effects of therapeutic NPs as antifibrillation agents, we probed the effects of a biomolecular corona derived from human CSF and/or plasma on Aβ fibrillation. The results demonstrated that the type of biomolecular corona can dictate the inhibitory or acceleratory effect of NPs on Aβ1-42 and Aβ25-35 fibrillation processes. More specifically, we found that the plasma biomolecular-corona-coated gold NPs, with sphere and rod shapes, has less inhibitory effect on Aβ1-42 fibrillation kinetics compared with CSF biomolecular-corona-coated and pristine NPs. Opposite results were obtained for Aβ25-35 peptide, where the pristine NPs accelerated the Aβ25-35 fibrillation process, whereas corona-coated ones demonstrated an inhibitory effect. In addition, the CSF biomolecular corona had less inhibitory effect than those obtained from plasma. Copyright © 2018 American Chemical Society.