Elucidating the Molecular Mechanisms of Amyloid Formation In Vitro and In Situ: A Challenge for Biophysics
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".
Deadline for manuscript submissions: closed (15 April 2024) | Viewed by 150
Special Issue Editors
Interests: protein aggregations; protein folding, misfolding and aggregation; spectroscopy methods
Interests: protein stability; amyloid aggregation; structure-function relation; aggregation of recombinant proteins; protein-protein and protein-ligand interactions
Special Issue Information
Dear Colleagues,
A great variety of human pathologies, including Alzheimer's and Parkinson's diseases and systemic amyloidosis, are associated with the misfolding and self-assembly of soluble proteins or peptides into insoluble aggregates. The mechanisms by which proteins convert from their functional forms into the amyloid state are highly complex and the process is known to depend on both the intrinsic characteristics of the protein and the environmental conditions under which aggregation occurs.
In this regard, several biophysical approaches have been developed to investigate protein aggregation not only in vitro but also within complex biological systems, thus contributing to shedding new light on how the protein aggregation behavior may be modulated in vivo.
This Special Issue will be focused on the application of biophysical methods, from low to high structural and spatial resolutions, to obtain complementary information on the aggregation process and on the structural features of the protein assemblies.
Dr. Antonino Natalello
Dr. Diletta Ami
Guest Editors
Manuscript Submission Information
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Keywords
- amyloid
- biophysics
- calorimetry
- ex-vivo
- in-situ
- mass spectrometry
- microscopy
- protein aggregation
- protein misfolding
- spectroscopy
