Understanding Amyloid Structures and Disease: A Continuing Challenge in Health Research
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 (28 February 2021) | Viewed by 31796
Special Issue Editor
Interests: metabolic biochemistry; thyroid hormone analogs and metabolites; vitamin D analogs; drug design, synthesis and development
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and deposition into plaques and intracellular inclusions is the hallmark of amyloid disease. Amyloidosis occurs in association with many pathological conditions that may be also linked to aging, such as Alzheimer's disease, Parkinson's disease, type II diabetes, and dialysis-related amyloidosis.
Amyloidogenic proteins are relatively small, typically soluble, and intrinsically disordered proteins that undergo remarkable conformational re-arrangements associated with a process of aggregation and self‐assembly that leads ultimately to the formation of fibrillar aggregates designated as amyloid fibrils. Even though recent years have witnessed an increasing interest in the self‐assembly of amyloidogenic proteins, with growing numbers of multidisciplinary scientific approaches (including experimental, theoretical, and computational tools), the elucidation of the atomic structure of amyloid fibrils formed from their intact protein precursors and the mechanisms relating fibril formation to disease have remained elusive.
Over the last few decades, there have been extensive efforts to develop novel inhibitors and modulators as potential therapeutics for amyloidogenic protein aggregation and the development of amyloid disease. Up to the present, however, drug therapies have been used to provide almost exclusively symptomatic benefits, but have failed to prevent or delay the onset of the disease. Therefore, there is a sense that therapeutic innovation is needed in order to effectively address the development and progression of the great diversity of amyloid diseases.
In this Special Issue, “Understanding amyloid structures and disease: a continuing challenge in health research,” we invite investigators to contribute original research articles and review articles to advance our knowledge in the molecular mechanisms of amyloidogenic protein aggregation and activity, as well as to provide new insights on the development of new therapeutic strategies for the prevention of amyloid diseases. It is our hope that this Special Issue will assist current and future generations of scientists in translating scientific findings into new treatments to effectively delay the onset or slow the progression of amyloid diseases.
Dr. Grazia Chiellini
Guest Editor
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