IMR Press / FBL / Special Issues / protein_folding

Protein Folding, Design and Aggregation: New Aspects and Uses

Submission deadline: 31 March 2023
Special Issue Editors
  • Eva Zerovnik, PhD
    Interests: protein folding; protein aggregation; amyloid; Alzheimer’s disease; protein oligomers toxicity; autophagy; cystatins
  • Ajda Taler-Vercic, PhD
    Institute of biochemistry and molecular genetics, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia
    Interests: amyloid fibril formation; iodine metabolism; thyroid; protein stability and interactions; biochemical diagnostics; structural biology
Special Issue Information

Dear Colleagues,

Proper protein folding is at the route of all life. Among others, proteins and peptides function as enzymes, hormones, neurotransmitters, scaffold for the cytoskeleton, and helpers for other proteins to fold. Conversely, protein mis-folding, aggregation and amyloid fibril formation cause many diseases. They span from systemic amyloidosis to other more local disorders, including those affecting the brain and peripheral neural system, such as Alzheimer’s disease, Parkinson’s disease and amyotrophic lateral sclerosis (ALS). The enormous impact neurodegenerative diseases have on society is well known. For example, Alzheimer’s disease affects 55 million people worldwide and is the seventh leading cause of death, carrying a significant impact on life quality of among older people.

A prerequisite for novel therapies of neurodegenerative diseases is understanding the pathological mechanisms in cells, including neurons, astrocytes and glia, which start the detrimental cascade of events that ultimately lead to chronic brain inflammation, oxidative stress and neurodegeneration. Impact of normal aging as a risk factor can be part of the studies. As well, the impact of viral or bacterial infections on protein aggregation or impaired aggregate clearance is highly relevant, particularly in light of the recent COVID pandemic.

Second, understanding and managing protein folding have important roles in preventing protein aggregation in pharmaceutical preparations of biological medicines, including antibodies. Systemic biology aims to design proteins with special properties that can also be used as inhibitors of other proteins’ aggregation or to inhibit viral spread by providing common epitopes.

Accordingly, the goal of this issue is to collect articles on any aspect of protein folding. This can comprise the following topics:

Designed proteins and wishful properties; stability and dynamics;

Kinetics, transition states and folding intermediates;

The role and action of chaperones;

Aggregation to amyloid-fibrils;

Mechanisms of aggregate clearance;

Influence of low complexity regions to protein aggregation and condensation;

Interaction of presumably toxic oligomers with biological membranes;

Formation of membraneless organelles.

Part of the studies could use large-scale -omics techniques, such as proteomics, genomics, metabolomics and epigenetics (epigenomics) to find common subscripts (biological markers) of the pathways involved in protein mis-folding, oligomerization, condensation, and irreversible aggregates formation.

Prof. Eva Žerovnik and Assis. Prof. Ajda Taler-Vercic

Guest Editors

protein folding
protein design
protein aggregation
molecular mechanisms of protein oligomerization and aggregation
protein condensation
aggregate toxicity
aggregate clearance
interaction of prefibrillar oligomers with membranes
markers of protein mis-folding
markers of oxidative stress
Manuscript Submission Information

Manuscripts should be submitted via our online editorial system at by registering and logging in to this website. Once you are registered, click here to start your submission. Manuscripts can be submitted now or up until the deadline. All papers will go through peer-review process. Accepted papers will be published in the journal (as soon as accepted) and meanwhile listed together on the special issue website. Research articles, reviews as well as short communications are preferred. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office to announce on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts will be thoroughly refereed through a double-blind peer-review process. Please visit the Instruction for Authors page before submitting a manuscript. The Article Processing Charge (APC) in this open access journal is 2500 USD. Submitted manuscripts should be well formatted in good English.

Published Paper (1 Paper)
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