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Special Issue "The Role of Environment in Amyloid Aggregation"

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: 28 February 2021.

Special Issue Editor

Dr. Vytautas Smirnovas
Website
Guest Editor
Institute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania
Interests: protein misfolding; protein aggregation; amyloid; prion; proteinaceous infectivity

Special Issue Information

Dear Colleagues,

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
Guest Editor

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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein misfolding
  • protein aggregation
  • amyloid
  • anti-amyloid compounds
  • amyloid polymorphism
  • prion
  • protein folding and stability
  • neurodegenerative diseases
  • aggregation kinetics
  • drug discovery

Published Papers

This special issue is now open for submission.
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