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Protein Aggregation and Proteinopathies
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Protein Aggregation and Proteinopathies

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 June 2025 | Viewed by 3676

Special Issue Editor

Prof. Dr. Hongyu Hu

E-Mail Website
Guest Editor
Biochemistry and Molecular Biology, Key Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, China
Interests: protein aggregation; protein interaction; proteinopathy; cellular homeostasis; RNA-binding protein; cellular biochemistry; biochemical techniques; biophysical techniques

Special Issue Information

Dear Colleagues,

The hallmark of some neurodegenerative diseases is the aggregation of abnormal proteins and the formation of inclusion bodies in neural cells. This Special Issue focuses on the mechanism of protein misfolding, amyloidogenic aggregation and sequestration, and phase transition of the disease-related proteins. The topics included in this Special Issue are as follows:

  • Mechanism of protein misfolding, aggregation and inclusion formation, phase transition, and their cellular effects;
  • Amyloidogenic disease-related proteins, especially polyglutamine proteins and RNA-binding proteins;
  • Sequestration of cellular essential proteins by the protein aggregates, and its pathological consequences;
  • Proteostasis network of the amyloidogenic proteins associated with proteinopathies;
  • Protein co-aggregation and co-pathologies;
  • Structural basis for and functional annotation of protein aggregation and sequestration.

Prof. Dr. Hongyu Hu
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein aggregation
  • inclusion
  • sequestration
  • interaction
  • phase transition
  • proteostasis
  • proteinopathy

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Published Papers (2 papers)

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Research

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12 pages, 1925 KiB  
Article
The Detection of Toxic Amyloid-β Fibril Fragments Through a Surface Plasmon Resonance Immunoassay
by Marten Beeg, Beatrice Rocutto, Elisabetta Battocchio, Letizia Dacomo, Alessandro Corbelli, Fabio Fiordaliso, Claudia Balducci and Marco Gobbi
Int. J. Mol. Sci. 2024, 25(23), 13020; https://doi.org/10.3390/ijms252313020 - 4 Dec 2024
Viewed by 888
Abstract
Amyloid-β1–42 (Aβ42) forms highly stable and insoluble fibrillar structures, representing the principal components of the amyloid plaques present in the brain of Alzheimer’s disease (AD) patients. The involvement of Aβ42 in AD-associated neurodegeneration has also been demonstrated, in particular for smaller and soluble [...] Read more.
Amyloid-β1–42 (Aβ42) forms highly stable and insoluble fibrillar structures, representing the principal components of the amyloid plaques present in the brain of Alzheimer’s disease (AD) patients. The involvement of Aβ42 in AD-associated neurodegeneration has also been demonstrated, in particular for smaller and soluble aggregates (oligomers). Based on these findings and on genetic evidence, Aβ42 aggregates are considered key players in the pathogenesis of AD and targets for novel therapies. Different approaches are currently used to detect the various aggregation states of Aβ peptide, including spectrophotometric methods, imaging techniques, and immunoassays, but all of these have specific limitations. To overcome them, we have recently exploited the peculiar properties of surface plasmon resonance (SPR) to develop an immunoassay capable of selectively detecting monomers and oligomers, discriminating them also from bigger fibrils in a mixture of different aggregated species, without any manipulation of the solution. In the present study, we extended these previous studies, showing that the SPR-based immunoassay makes it possible to unveil the fibril fragmentation induced mechanically, a result difficult to be conveniently and reliably assessed with other approaches. Moreover, we show that SPR-recognized fibril fragments are more toxic than the larger fibrillar structures, suggesting the relevance of the proposed SPR-based immunoassay. Full article
(This article belongs to the Special Issue Protein Aggregation and Proteinopathies)
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Review

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28 pages, 1761 KiB  
Review
Co-Aggregation of TDP-43 with Other Pathogenic Proteins and Their Co-Pathologies in Neurodegenerative Diseases
by Lei-Lei Jiang, Xiang-Le Zhang and Hong-Yu Hu
Int. J. Mol. Sci. 2024, 25(22), 12380; https://doi.org/10.3390/ijms252212380 - 18 Nov 2024
Cited by 1 | Viewed by 2410
Abstract
Pathological aggregation of a specific protein into insoluble aggregates is a common hallmark of various neurodegenerative diseases (NDDs). In the earlier literature, each NDD is characterized by the aggregation of one or two pathogenic proteins, which can serve as disease-specific biomarkers. The aggregation [...] Read more.
Pathological aggregation of a specific protein into insoluble aggregates is a common hallmark of various neurodegenerative diseases (NDDs). In the earlier literature, each NDD is characterized by the aggregation of one or two pathogenic proteins, which can serve as disease-specific biomarkers. The aggregation of these specific proteins is thought to be a major cause of or deleterious result in most NDDs. However, accumulating evidence shows that a pathogenic protein can interact and co-aggregate with other pathogenic proteins in different NDDs, thereby contributing to disease onset and progression synergistically. During the past years, more than one type of NDD has been found to co-exist in some individuals, which may increase the complexity and pathogenicity of these diseases. This article reviews and discusses the biochemical characteristics and molecular mechanisms underlying the co-aggregation and co-pathologies associated with TDP-43 pathology. The TDP-43 aggregates, as a hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), can often be detected in other NDDs, such as Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD) and spinocerebellar ataxia type 2 (SCA2). In many cases, TDP-43 is shown to interact and co-aggregate with multiple pathogenic proteins in vitro and in vivo. Furthermore, the co-occurrence and co-aggregation of TDP-43 with other pathogenic proteins have important consequences that may aggravate the diseases. Thus, the current viewpoint that the co-aggregation of TDP-43 with other pathogenic proteins in NDDs and their relevance to disease progression may gain insights into the patho-mechanisms and therapeutic potential of various NDDs. Full article
(This article belongs to the Special Issue Protein Aggregation and Proteinopathies)
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