Special Issue "Regulation of Functional Protein Aggregation: From Amyloids to Biomaterials"
Deadline for manuscript submissions: 30 June 2021.
Interests: membrane transport; lipids; lipid droplets; lipidomics; liver fibrosis; liver regeneration; hepatic stellate cells; retinoids; functional amyloids; CAP superfamily proteins
Interests: protein-protein interactions; protein aggregation; autophagy; reproduction
Interests: protein folding and Aggregation; Tau; heat shock proteins; chaperones
Numerous proteins and peptides have the capacity to self‐assemble into amyloid fibrils that are characterized by β-sheet polymer structures. Amyloid assembly has long been associated with many devastating human diseases, such as Alzheimer’s, Parkinson’s, diabetes type 2, and ALS.
Strikingly, amyloid folds with their remarkable, multifaceted appearance are also present in nature and occurring in various physiologically forms as so-called “functional amyloids”. They appear in fungi, insects, archaea, bacteria, and humans. Functional amyloids are often characterized by their reversible nature, unlike the extremely stable pathological amyloid fibrils. In addition, their presence requires careful biophysical control to avoid potentially harmful effects. This strongly suggests that functional amyloid assemblies are subject to strict regulation, leading to the formation of correct ‘sub’-structures to prevent toxicity and allowing reversal of amyloid assembly. Likewise, amyloid formation may be linked to liquid–liquid phase separation. The concept that is emerging is that amyloidic β-sheet folds can perform a multitude of biological functions. Rapid progress in the field of protein amyloid assembly now offers highly exciting new opportunities to unravel the secrets of amyloid formation. This will not only benefit the understanding of the role of functional and pathological amyloids in health and disease but will also promote innovation in bioengineering. The unique chemical characteristics of amyloidogenic proteins can be used to develop brand new materials for biofilm, biosensor, bioelectronic, and biomedical applications.
This Special Issue calls for original research in basic science and translational research, as well as for reviews and perspectives that address the existence, regulation, and role of functional amyloids in the physiology of organisms. In addition, contributions that describe progress to create new biomaterials based on β-sheet assemblies are welcomed.
Prof. Dr. J.B. Helms,
Dr. Dora V. Kaloyanova
Dr. Stefan Rüdiger
Manuscript Submission Information
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- Protein aggregation
- β-sheet fold
- Protein fibrils
- Functional amyloids