Special Issue "The Role of Environment in Amyloid Aggregation"
Deadline for manuscript submissions: 28 February 2021.
Interests: protein misfolding; protein aggregation; amyloid; prion; proteinaceous infectivity
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
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
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- protein misfolding
- protein aggregation
- anti-amyloid compounds
- amyloid polymorphism
- protein folding and stability
- neurodegenerative diseases
- aggregation kinetics
- drug discovery