Special Issue "The Role of Environment in Amyloid Aggregation"
Deadline for manuscript submissions: closed (31 August 2021) | Viewed by 13660
Interests: protein misfolding; protein aggregation; amyloid; prion; proteinaceous infectivity
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The ability to form amyloid structures may be a generic property of polypeptides, and there are two major factors which define the probability of amyloid fibril formation—amino acid sequence of the protein/peptide and the environmental conditions. In the case of folded proteins, at least partial unfolding is necessary to trigger the amyloid formation pathway, so increased temperature, extreme pH conditions, addition of denaturants or any other changes in the environment leading to destabilization of protein structure are used in amyloid aggregation studies. Even in the case of disordered proteins, neutralization of charges or contact with hydrophobic surfaces may be necessary to induce amyloid formation. In addition to the specific conditions required for amyloid formation, changes in the environment may alter the mechanism of aggregation and lead to distinct amyloid fibril conformations. Finally, environment conditions affect the kinetics of aggregation and may alter the effect of anti-amyloid compounds.
The value of protein amyloid studies in vitro for health/pharma industry is limited, as extrapolation of the results toward amyloid formation in cells and organisms is not precise. The precision of extrapolation could increase with comprehensive knowledge of how the broad range of environmental conditions affect protein amyloid aggregation. It is my belief that to increase the value of our research, we must collect more data and periodically overview and condense them. Thus, I would like to invite you to share your knowledge and data on protein aggregation at different conditions and submit research or review articles to this issue.
Dr. Vytautas Smirnovas
Manuscript Submission Information
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- protein misfolding
- protein aggregation
- anti-amyloid compounds
- amyloid polymorphism
- protein folding and stability
- neurodegenerative diseases
- aggregation kinetics
- drug discovery