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    Graphene-based nanoparticles as potential treatment options for parkinson’s disease: A molecular dynamics study

    , Article International Journal of Nanomedicine ; Volume 15 , 2020 , Pages 6887-6903 Alimohammadi, E ; Khedri, M ; Jahromi, A. M ; Maleki, R ; Rezaian, M ; Sharif University of Technology
    Dove Medical Press Ltd  2020
    Introduction: The study of abnormal aggregation of proteins in different tissues of the body has recently earned great attention from researchers in various fields of science. Concerning neurological diseases, for instance, the accumulation of amyloid fibrils can contribute to Parkinson’s disease, a progressively severe neurodegenerative disorder. The most prominent features of this disease are the degeneration of neurons in the substantia nigra and accumulation of α-synuclein aggregates, especially in the brainstem, spinal cord, and cortical areas. Dopamine replacement therapies and other medications have reduced motor impairment and had positive consequences on patients’ quality of life.... 

    Design and Fabrication of Drug-loaded Nanoparticles to Prevent Fibrillation of Alpha-synuclein in Parkinson

    , M.Sc. Thesis Sharif University of Technology Nayebzadeh, Ramin (Author) ; Mashayekhan, Shohreh (Supervisor) ; Morshedi, Dina (Supervisor)
    The purpose of this study is to assess the inhibitory effects of an appropriate nanoparticles loaded with gallic acid on the fibrillation of alpha-synuclein. Alpha-synuclein is a major component of protein plaques in synucleinopathies, particularly Parkinson’s disease. Gallic acid (GA, 3,4,5-trihydroxy benzoic acid) is a well–known small molecule which can inhibit the formation of α-synuclein fibrils. For the process of fibrillation, purified protein was incubated at 37◦C and pH 7.2. Fibrillation was analyzed by the standard fibril methods.after that investigated fabricating of gallic acid trapped in the chitosan nanoparticles and gallic acid loaded in chitosan –coated mesoporous silica... 

    Curcumin-loaded amine-functionalized mesoporous silica nanoparticles inhibit α-synuclein fibrillation and reduce its cytotoxicity-associated effects

    , Article Langmuir ; Volume 32, Issue 50 , 2016 , Pages 13394-13402 ; 07437463 (ISSN) Taebnia, N ; Morshedi, D ; Yaghmaei, S ; Aliakbari, F ; Rahimi, F ; Arpanaei, A ; Sharif University of Technology
    American Chemical Society  2016
    This study aimed to develop a drug carrier based on amine-functionalized mesoporous silica nanoparticles (AAS-MSNPs) for a poorly water-soluble drug, curcumin (CUR), and to study its effects on α-synuclein (α-Syn) fibrillation and cytotoxicity. Here, we show that AAS-MSNPs possess high values of loading efficiency and capacity (33.5% and 0.45 mg drug/mg MSNPs, respectively) for CUR. It is also revealed that α-Syn species interact strongly with the CUR-loaded AAS-MSNPs, leading to a significant inhibition of the fibrillation process. Furthermore, these samples reduce the toxic effects of CUR. However, drug-loaded AAS-MSNPs do not affect the cytotoxic properties of the formed fibrils... 

    The hot sites of α-synuclein in amyloid fibril formation

    , Article Scientific Reports ; Volume 10, Issue 1 , 22 July , 2020 Khammari, A ; Arab, S. S ; Ejtehadi, M. R ; Sharif University of Technology
    Nature Research  2020
    The role of alpha-synuclein (αS) amyloid fibrillation has been recognized in various neurological diseases including Parkinson’s Disease (PD). In early stages, fibrillation occurs by the structural transition from helix to extended states in monomeric αS followed by the formation of beta-sheets. This alpha-helix to beta-sheet transition (αβT) speeds up the formation of amyloid fibrils through the formation of unstable and temporary configurations of the αS. In this study, the most important regions that act as initiating nuclei and make unstable the initial configuration were identified based on sequence and structural information. In this regard, a Targeted Molecular Dynamics (TMD)... 

    Mechanistic understanding of the interactions between nano-objects with different surface properties and α-synuclein

    , Article ACS Nano ; Volume 13, Issue 3 , 2019 , Pages 3243-3256 ; 19360851 (ISSN) Mohammad Beigi, H ; Hosseini, A ; Adeli, M ; Ejtehadi, M. R ; Christiansen, G ; Sahin, C ; Tu, Z ; Tavakol, M ; Dilmaghani Marand, A ; Nabipour, I ; Farzadfar, F ; Otzen, D. E ; Mahmoudi, M ; Hajipour, M. J ; Sharif University of Technology
    American Chemical Society  2019
    Aggregation of the natively unfolded protein α-synuclein (α-syn) is key to the development of Parkinson's disease (PD). Some nanoparticles (NPs) can inhibit this process and in turn be used for treatment of PD. Using simulation strategies, we show here that α-syn self-assembly is electrostatically driven. Dimerization by head-to-head monomer contact is triggered by dipole-dipole interactions and subsequently stabilized by van der Waals interactions and hydrogen bonds. Therefore, we hypothesized that charged nano-objects could interfere with this process and thus prevent α-syn fibrillation. In our simulations, positively and negatively charged graphene sheets or superparamagnetic iron oxide...