Oxidative Folding of Proteins and Peptides
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".
Deadline for manuscript submissions: closed (15 April 2021) | Viewed by 36436
Special Issue Editor
Interests: selenium chemistry; protein chemistry
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Dear Colleagues,
Since the pioneering work by Dr. Christian Anfinsen—a 1972 Nobel Laureate in Chemistry—in the 1960s, researchers have devoted many efforts to compiling experimental and theoretical outcomes from protein folding studies in the literature. In earlier years, such studies were focused on reproducing the process of protein folding in vitro to observe the transiently generated intermediates. As a result, the major folding pathways were characterized for several disulfide-containing proteins, such as bovine pancreatic trypsin inhibitor (BPTI) and ribonuclease A (RNase A). However, the general principle of protein folding, which can be applied to a variety of proteins, has not yet been elucidated.
On the other hand, oxidative protein folding in vivo has also been studied in depth in the last few decades. While a protein with disulfide bonds slowly gains its native structure in vitro under suitable redox conditions, this spontaneous process is controlled in vivo by various intracellular factors, such as protein disulfide isomerase (PDI) and molecular chaperons, which allow the protein to fold to its native structure in a short time. Proteins fold inside a cellular organelle, called endoplasmic reticulum (ER), but this oxidation process would also generate misfolded polypeptides (or non-natural species with scrambled disulfide bonds) in a certain ratio. The produced toxic misfolded species, however, can be reduced with the aid of other factors and returned to the regular folding process again. The structures and functional mechanisms of these factors remain largely unknown.
Recently, new experimental methodologies have been devised and successfully applied to various disulfide-containing proteins. For example, new folding reagents and artificial model peptides have been developed to elucidate the oxidative folding pathways in vitro in more detail. Structural and functional analyses of the factor proteins, which are involved in the oxidative protein folding in vivo, have been elaborated to promote our understanding of oxidative protein folding. These factors were also found to be relevant to protein misfolding diseases.
In this Special Issue of Molecules, original research articles as well as reviews in related research areas, namely oxidative folding of protein and peptides, are cordially invited.
Prof. Dr. Michio Iwaoka
Guest Editor
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Keywords
- Disulfide formation and rearrangement
- Folding mechanisms
- In-cell folding
- Protein misfolding
- Artificial peptides and proteins
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