Therapeutic Development towards Protein Misfolding Diseases
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: closed (31 May 2022) | Viewed by 7744
Special Issue Editors
Interests: amyloid; protein aggregation; protein misfolding; neurodegenerative diseases; peptide self assembly; peptide synthesis; amyloid inhibitors
Special Issue Information
Dear Colleagues,
Both the self-assembly and aggregation of misfolded proteins are associated with many medical disorders, including Alzheimer’s, Parkinson’s, type-2 diabetes and certain types of cancer diseases. The onset of aggregation of the diseased proteins is not completely understood. Despite their structural and sequential differences, various diseased proteins self-assemble to form amyloid fibrils, which are intriguingly very similar in their morphology, conformation (increased content of beta structures) and properties in terms of binding specific dyes (for example, thioflavin T and Congo red). There are various factors that influence the aggregation such proteins, including sequence of the protein, post-translational modification, the presence of molecular crowding or other biomolecules (such as lipids, glycan and proteins), in addition to the pH and temperature of the environment.
Thus, it is essential to develop effective therapeutic strategies to mitigate protein aggregation and the diseases associated with this.
Dr. Ashim Paul
Dr. Moran Frenkel-Pinter
Guest Editors
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Keywords
- protein misfolding diseases
- neurodegenerative diseases
- protein aggregation amyloid
- amyloid inhibitors
- small molecules
- post-translational modifications
- antibody
- drug development
- beta-sheet breaker peptide
- peptidomimetics
- antibody mimetics
- blood–brain barrier
- molecular chaperones
- mechanism of aggregation
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