Special Issue "Alzheimer's Amyloid: Structure, Function, and Disease"
A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".
Deadline for manuscript submissions: closed (30 August 2023) | Viewed by 2043
Special Issue Editors
Interests: structural biology; computational biology; protein crystallography; molecular modeling; molecular docking; drug design; molecular dynamics
Special Issues, Collections and Topics in MDPI journals
Interests: Alzheimer’s disease; prion diseases; amyloidogenesis; inhibitors of amyloidogenesis; amyloid fibrils
Special Issue Information
Dear Colleagues,
Alzheimer’s disease (AD), a fatal neurodegenerative disease, has puzzled the scientific community for over a century. AD currently affects 50 million patients and is estimated to reach 152 million in 2050. The COVID-19 pandemic may have significantly increased these estimates according to an alarming report showing a hazard ratio of 1.69 for new-onset AD in older people as a late sequel of COVID-19. This may substantially increase the already enormous burden on public health budgets, health care and older people and societies. Therefore, despite the controversial approval of an expensive therapy with aducanumab and expected approval of the use of monoclonal antibodies against β-amyloid, there is an urgent need to find cheap and effective small-molecule treatments for this disease. For this Special Issue, we welcome studies concerning inhibitors of β-amyloid aggregation into oligomers and mature fibrils as well as compounds dissolving mature fibrils. Computational studies docking new compounds to β-amyloid monomers, oligomers and fibrils and molecular dynamics experiments alone or preliminary to “wet” biochemistry leading to elucidation of the mechanism underlying the inhibition of aggregation or dissolution of fibrils are also encouraged.
Dr. Adam Jarmuła
Dr. Dariusz Stępkowski
Guest Editors
Manuscript Submission Information
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Keywords
- Alzheimer’s disease
- beta-amyloid
- in silico studies
- amyloidogenesis
- inhibition of fibrillation
- dissolution of amyloid fibrils