Understanding Protein/Peptide Self-Assembly using Structural and Biophysical Chemistry

Dear Colleagues,

Protein and peptide self-assembly is an emerging area of research at the triple point where chemistry, biology, and physics meet.
Protein self-assembly makes up functional superstructures in living cells. These organized three-dimensional nano- and microstructures are built up by the information encoded in single amino acids and tuned by environmental stimuli. It is also accepted that misfolding and self-assembly of proteins and peptides into more complex supramolecular structures such as amyloid oligomers, protofilaments, and fibrils are associated with different pathogenesis like prion or Alzheimer’s diseases, among others. Finally, the secondary transition and self-assembling of peptides into gels, fibrils, fibers, tubules, or sheets have found applications in tissue engineering and biomedical devices. In this context, the control of these functional biomaterials triggered by an external stimulus such as temperature, pH, or mechanical forces is highly desired.

The purpose of this Special Issue is to show the power of biophysical chemistry in combination with other areas of chemistry, like peptide chemistry, the design of sensors of peptide self-assembly, or molecular modeling to elucidate at the molecular level the process of self-assembly in proteins and peptides. Additionally, advances in understanding protein/peptide self-assembly from a soft matter perspective are particularly welcome, as well as multidisciplinary studies offering new principles, strategies, and insights. Contributions to this Special Issue, both in the form of original research or review articles that favor the advance of this fascinating area of research, are cordially invited.

Dr. Veronica Dodero
Guest Editor

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