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
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- Open Access Original ResearchAmyloid Formation of Stefin B Protein Studied by Infrared SpectroscopyUrban Novak, Eva Žerovnik, Ajda Taler-Verčič, MagdaTušek Žnidarič, ... Jože GrdadolnikFront. Biosci. (Landmark Ed) 2023, 28(3), 46; https://doi.org/10.31083/j.fbl2803046(This article belongs to the Special Issue Protein Folding, Design and Aggregation: New Aspects and Uses)36Downloads76Views