Amyloid Formation - From Molecular Mechanisms to Disease and Novel Nanomaterials

Ordered protein aggregation, known as amyloid formation, has recently emerged as a universal phenomenon due to extensive research in protein folding and amyloid diseases. The amyloid is viewed as a generic structure characterized by a cross-ß-sheet formation in its core, which implies that any polypeptide can adopt this conformation under amyloid-prone conditions. Deciphering the molecular mechanisms of amyloid formation is of paramount importance due to their involvement in very wide range of phenomena, from amyloid diseases to nanomaterials. Indeed, amyloid deposits are involved in a wide range of human pathologies, including Alzheimer's and Parkinson's diseases, diabetes mellitus, systemic amyloidosis and others.

Amyloids also represent a new challenge for industry, which relies on proteinaceous products such as biopharmaceuticals. The potentially hazardous properties of amyloids demand the highest attention and in-depth analysis in order to provide safe and sure products. Some other properties of amyloids, such as their remarkable physical stability, can be applied in nanotechnology for the fabrication of novel nano-sized structures with controlled parameters. The cytotoxicity of proteinaceous complexes can also be used as a double-edged sword,  either killing normal cells or inducing the death of unwanted tumor cells depending on the conditions.

You are very welcome to submit your research within the broad range of topics regarding the molecular mechanisms governing amyloid formation and leading to the development of amyloid disease or the production of novel nanomaterials.

Prof. Dr. Ludmilla Morozova-Roche
Guest Editor

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• amyloid
• protein misfolding
• amyloid disease
• nanomaterial
• fibrils
• oligomers
• intermediate states
• self-assembly
• mechanisms