Protein Aggregation: Molecular Mechanisms, Determinants and Therapeutic Approaches Volume II
A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Cell Biology and Pathology".
Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 313
Special Issue Editor
Interests: molecular biophysics; structural biology; structural bioinformatics; cellular biophysics; computational biology; protein structure and stability; protein misfolding; protein aggregation; amyloid formation; functional amyloids; aggregation-prone regions; neurodegenerative disorders
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Macromolecular protein assemblies including protein aggregates, biomolecular condensates, and ordered amyloid fibril formation have been associated with various widespread diseases, spanning from major neurodegenerative disorders to certain forms of cancer. At the same time, amyloid formation has also been shown to support important biological functions starting from humans and extending to single-cell organisms. The recent efflux of structural information on amyloid architecture, combined with studies on the molecular determinants and mechanisms that promote self- and heterotypic assembly, has highlighted certain unresolved properties of protein aggregates, such as structural polymorphism and its differential association to disease, selective vulnerability of specific cell types to certain toxic aggregate species, and complex spreading patterns, while also promoting the design of novel therapeutic approaches against this group of diseases.
MDPI’s Biomedicines is setting up this Special Issue aiming to promote new findings focused on the current understanding of the molecular mechanisms and/or the determinants of macromolecular protein assemblies in both disease and in function, whether that is the formation of functional amyloids or the development of new aggregation-based technologies and strategies for therapeutics and nanomaterials. Our interest extends to studies that uncover new aspects of the cross-interaction interplay of protein assemblies with other biomolecules (e.g., nucleic acids, proteins, lipids) and the role of other factors in this process (pH, salts, post-translational modifications, and more). We aim to highlight recent advances in understanding the structural diversity of protein assemblies spanning from phase-separated biomolecular condensates to oligomers and polymorphic end-state amyloid fibrils and their interplay with proteostatic control mechanisms that regulate their formation and balance in a cellular context.
Dr. Nikolaos N. Louros
Guest Editor
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Keywords
- protein aggregation
- functional amyloids
- macromolecular protein assembly
- cellular mechanisms of assembly
- sequence/structure determinants
- phase separation
- biomolecular cross-interactions in aggregation
- role of external factors in aggregation
- amyloid polymorphism
- design of functional aggregates
- aggregation-based technologies and therapeutics
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