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  1. Article ; Online: 14-3-3τ as a Modulator of Early α-Synuclein Multimerization and Amyloid Formation.

    Heesink, Gobert / van den Oetelaar, Maxime C M / Semerdzhiev, Slav A / Ottmann, Christian / Brunsveld, Luc / Blum, Christian / Claessens, Mireille M A E

    ACS chemical neuroscience

    2024  

    Abstract: The aggregation of α-synuclein (αS) plays a key role in Parkinson's disease (PD) etiology. While the onset of PD is age-related, the cellular quality control system appears to regulate αS aggregation throughout most human life. Intriguingly, the protein ... ...

    Abstract The aggregation of α-synuclein (αS) plays a key role in Parkinson's disease (PD) etiology. While the onset of PD is age-related, the cellular quality control system appears to regulate αS aggregation throughout most human life. Intriguingly, the protein 14-3-3τ has been demonstrated to delay αS aggregation and the onset of PD in various models. However, the molecular mechanisms behind this delay remain elusive. Our study confirms the delay in αS aggregation by 14-3-3τ, unveiling a concentration-dependent relation. Utilizing microscale thermophoresis (MST) and single-molecule burst analysis, we quantified the early αS multimers and concluded that these multimers exhibit properties that classify them as nanoscale condensates that form in a cooperative process, preceding the critical nucleus for fibril formation. Significantly, the αS multimer formation mechanism changes dramatically in the presence of scaffold protein 14-3-3τ. Our data modeling suggests that 14-3-3τ modulates the multimerization process, leading to the creation of mixed multimers or co-condensates, comprising both αS and 14-3-3τ. These mixed multimers form in a noncooperative process. They are smaller, more numerous, and distinctively not on the pathway to amyloid formation. Importantly, 14-3-3τ thus acts in the very early stage of αS multimerization, ensuring that αS does not aggregate but remains soluble and functional. This offers long-sought novel entries for the pharmacological modulation of PD.
    Language English
    Publishing date 2024-04-18
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.4c00100
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: SARS-CoV-2 N-protein induces the formation of composite α-synuclein/N-protein fibrils that transform into a strain of α-synuclein fibrils.

    Semerdzhiev, Slav A / Segers-Nolten, Ine / van der Schoot, Paul / Blum, Christian / Claessens, Mireille M A E

    Nanoscale

    2023  Volume 15, Issue 45, Page(s) 18337–18346

    Abstract: The presence of deposits of alpha-synuclein (αS) fibrils in the cells of the brain is a hallmark of several α-synucleinopathies, including Parkinson's disease. As most disease cases are not familial, it is likely that external factors play a role in the ... ...

    Abstract The presence of deposits of alpha-synuclein (αS) fibrils in the cells of the brain is a hallmark of several α-synucleinopathies, including Parkinson's disease. As most disease cases are not familial, it is likely that external factors play a role in the disease onset. One of the external factors that may influence the disease onset is viral infection. It has recently been shown in
    MeSH term(s) Humans ; alpha-Synuclein/metabolism ; SARS-CoV-2 ; COVID-19 ; Parkinson Disease/metabolism ; Brain/metabolism ; Amyloid/metabolism
    Chemical Substances alpha-Synuclein ; Amyloid
    Language English
    Publishing date 2023-11-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 2515664-0
    ISSN 2040-3372 ; 2040-3364
    ISSN (online) 2040-3372
    ISSN 2040-3364
    DOI 10.1039/d3nr03556e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: SARS-CoV-2 N-protein induces the formation of composite α-synuclein/N-protein fibrils that transform into a strain of α-synuclein fibrils

    Semerdzhiev, Slav A. / Segers-Nolten, Ine / Schoot, Paul van der / Blum, Christian / Claessens, Mireille M.A.E.

    bioRxiv

    Abstract: The presence of deposits of alpha-synuclein fibrils in cells of the brain are a hallmark of several α-synucleinopathies, including Parkinson9s disease. As most disease cases are not familial, it is likely that external factors play a role in disease ... ...

    Abstract The presence of deposits of alpha-synuclein fibrils in cells of the brain are a hallmark of several α-synucleinopathies, including Parkinson9s disease. As most disease cases are not familial, it is likely that external factors play a role in disease onset. One of the external factors that may influence disease onset are viral infections. It has recently been shown that in the presence of SARS-Cov-2 N-protein, αS fibril formation is faster and proceeds in an unusual two-step aggregation process. Here, we show that faster fibril formation is not due to a SARS-CoV-2 N-protein-catalysed formation of an aggregation-prone nucleus. Instead, aggregation starts with the formation of a population of mixed αS/N-protein fibrils with low affinity for αS. After the depletion of N-protein, fibril formation comes to a halt, until a slow transformation to fibrils with characteristics of pure αS fibril strains occurs. This transformation into a strain of αS fibrils subsequently results in a second phase of fibril growth until a new equilibrium is reached. Our findings point at the possible relevance of fibril strain transformation in the cell-to-cell spread of the αS pathology and disease onset.
    Keywords covid19
    Language English
    Publishing date 2023-03-13
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2023.03.13.532385
    Database COVID19

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  4. Article ; Online: Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.

    Semerdzhiev, Slav A / Fakhree, Mohammad A A / Segers-Nolten, Ine / Blum, Christian / Claessens, Mireille M A E

    ACS chemical neuroscience

    2021  Volume 13, Issue 1, Page(s) 143–150

    Abstract: First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson's disease (PD) have been reported. Currently, it is unclear if there is also a direct causal link between these diseases. To obtain first insights into ...

    Abstract First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson's disease (PD) have been reported. Currently, it is unclear if there is also a direct causal link between these diseases. To obtain first insights into a possible molecular relation between viral infections and the aggregation of α-synuclein protein into amyloid fibrils characteristic for PD, we investigated the effect of the presence of SARS-CoV-2 proteins on α-synuclein aggregation. We show, in test tube experiments, that SARS-CoV-2 spike protein (S-protein) has no effect on α-synuclein aggregation, while SARS-CoV-2 nucleocapsid protein (N-protein) considerably speeds up the aggregation process. We observe the formation of multiprotein complexes and eventually amyloid fibrils. Microinjection of N-protein in SH-SY5Y cells disturbed the α-synuclein proteostasis and increased cell death. Our results point toward direct interactions between the N-protein of SARS-CoV-2 and α-synuclein as molecular basis for the observed correlation between SARS-CoV-2 infections and Parkinsonism.
    MeSH term(s) Amyloid/metabolism ; COVID-19 ; Coronavirus Nucleocapsid Proteins/metabolism ; Humans ; Phosphoproteins/metabolism ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; alpha-Synuclein/metabolism
    Chemical Substances Amyloid ; Coronavirus Nucleocapsid Proteins ; Phosphoproteins ; Spike Glycoprotein, Coronavirus ; alpha-Synuclein ; nucleocapsid phosphoprotein, SARS-CoV-2 ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2021-12-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.1c00666
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils.

    van Dalen, Maurice C E / Vaneyck, Jonathan / Semerdzhiev, Slav A / Karperien, Marcel / Post, Janine N / Claessens, Mireille M A E

    Langmuir : the ACS journal of surfaces and colloids

    2021  Volume 37, Issue 24, Page(s) 7349–7355

    Abstract: Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. ... ...

    Abstract Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical applications the gels have to function in compositionally complex physiological solutions, their rheological behavior is typically only characterized in simple buffers. Here we show that the viscoelastic response of networks of amyloid fibrils of the protein lysozyme in biologically relevant solutions substantially differs from the response in simple buffers. We observe enhanced energy dissipation in both cell culture medium and synovial fluid. We attribute this energy dissipation to interactions of the amyloid fibrils with other molecules in these solutions and especially to the adsorption of the abundantly present protein serum albumin. This finding provides the basis for a better understanding of the performance of amyloid hydrogels in biomedical applications.
    MeSH term(s) Adsorption ; Amyloid ; Biocompatible Materials ; Hydrogels ; Muramidase
    Chemical Substances Amyloid ; Biocompatible Materials ; Hydrogels ; Muramidase (EC 3.2.1.17)
    Language English
    Publishing date 2021-06-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.1c00657
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Interactions between SARS-CoV-2 N-protein and α-synuclein accelerate amyloid formation

    Semerdzhiev, Slav / Fakhree, Mohammad Amin Abolghassemi / Segers-Nolten, Ine / Blum, Christian / Claessens, Mireille M.A.E.

    bioRxiv

    Abstract: First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson9s disease have been reported. Currently it is unclear if there also is a direct causal link between these diseases. To obtain first insights into a ... ...

    Abstract First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson9s disease have been reported. Currently it is unclear if there also is a direct causal link between these diseases. To obtain first insights into a possible molecular relation between viral infections and the aggregation of α-synuclein protein into amyloid fibrils characteristic for Parkinson9s disease, we investigated the effect of the presence of SARS-CoV-2 proteins on α synuclein aggregation. We show, in test tube experiments, that SARS-CoV-2 S-protein has no effect on α-synuclein aggregation while SARS-CoV-2 N-protein considerably speeds up the aggregation process. We observe the formation of multi-protein complexes, and eventually amyloid fibrils. Microinjection of N-protein in SHSY-5Y cells disturbed the α-synuclein proteostasis and increased cell death. Our results point toward direct interactions between the N-protein of SARS-CoV-2 and α-synuclein as molecular basis for the observed coincidence between SARS-CoV-2 infections and Parkinsonism.
    Keywords covid19
    Language English
    Publishing date 2021-04-12
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2021.04.12.439549
    Database COVID19

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  7. Article: Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils

    van Dalen, Maurice C. E. / Vaneyck, Jonathan / Semerdzhiev, Slav A. / Karperien, Marcel / Post, Janine N. / Claessens, Mireille M. A. E.

    Langmuir. 2021 June 07, v. 37, no. 24

    2021  

    Abstract: Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. ... ...

    Abstract Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical applications the gels have to function in compositionally complex physiological solutions, their rheological behavior is typically only characterized in simple buffers. Here we show that the viscoelastic response of networks of amyloid fibrils of the protein lysozyme in biologically relevant solutions substantially differs from the response in simple buffers. We observe enhanced energy dissipation in both cell culture medium and synovial fluid. We attribute this energy dissipation to interactions of the amyloid fibrils with other molecules in these solutions and especially to the adsorption of the abundantly present protein serum albumin. This finding provides the basis for a better understanding of the performance of amyloid hydrogels in biomedical applications.
    Keywords adsorption ; amyloid ; biocompatible materials ; cell culture ; culture media ; energy ; hydrogels ; lysozyme ; serum albumin ; synovial fluid ; viscoelasticity
    Language English
    Dates of publication 2021-0607
    Size p. 7349-7355.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.1c00657
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: Morphing of liquid crystal surfaces by emergent collectivity

    Hanne M. van der Kooij / Slav A. Semerdzhiev / Jesse Buijs / Dirk J. Broer / Danqing Liu / Joris Sprakel

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 9

    Abstract: Liquid crystal networks can morph their shape in response to electrical stimulus. Here the authors provide a detailed description of their deformation mechanism and introduce a method to observe the dynamic surface of liquid crystal elastomers. This ... ...

    Abstract Liquid crystal networks can morph their shape in response to electrical stimulus. Here the authors provide a detailed description of their deformation mechanism and introduce a method to observe the dynamic surface of liquid crystal elastomers. This could help with the development of smart materials.
    Keywords Science ; Q
    Language English
    Publishing date 2019-08-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Morphing of liquid crystal surfaces by emergent collectivity

    Hanne M. van der Kooij / Slav A. Semerdzhiev / Jesse Buijs / Dirk J. Broer / Danqing Liu / Joris Sprakel

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 9

    Abstract: Liquid crystal networks can morph their shape in response to electrical stimulus. Here the authors provide a detailed description of their deformation mechanism and introduce a method to observe the dynamic surface of liquid crystal elastomers. This ... ...

    Abstract Liquid crystal networks can morph their shape in response to electrical stimulus. Here the authors provide a detailed description of their deformation mechanism and introduce a method to observe the dynamic surface of liquid crystal elastomers. This could help with the development of smart materials.
    Keywords Science ; Q
    Language English
    Publishing date 2019-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Morphing of liquid crystal surfaces by emergent collectivity.

    van der Kooij, Hanne M / Semerdzhiev, Slav A / Buijs, Jesse / Broer, Dirk J / Liu, Danqing / Sprakel, Joris

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 3501

    Abstract: Liquid crystal surfaces can undergo topographical morphing in response to external cues. These shape-shifting coatings promise a revolution in various applications, from haptic feedback in soft robotics or displays to self-cleaning solar panels. The ... ...

    Abstract Liquid crystal surfaces can undergo topographical morphing in response to external cues. These shape-shifting coatings promise a revolution in various applications, from haptic feedback in soft robotics or displays to self-cleaning solar panels. The changes in surface topography can be controlled by tailoring the molecular architecture and mechanics of the liquid crystal network. However, the nanoscopic mechanisms that drive morphological transitions remain unclear. Here, we introduce a frequency-resolved nanostrain imaging method to elucidate the emergent dynamics underlying field-induced shape-shifting. We show how surface morphing occurs in three distinct stages: (i) the molecular dipoles oscillate with the alternating field (10-100 ms), (ii) this leads to collective plasticization of the glassy network (~1 s), (iii) culminating in actuation of the topography (10-100 s). The first stage appears universal and governed by dielectric coupling. By contrast, yielding and deformation rely on a delicate balance between liquid crystal order, field properties and network viscoelasticity.
    Language English
    Publishing date 2019-08-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-019-11501-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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