XRD1 Highlights

Heterochirality and Halogenation Control Phe-Phe Hierarchical Assembly

A series of Phe-Phe analogs were studied for self-assembly into nanotubes to offer new ways to design their chemical structure through a simple approach to exert control over the formation, size, and biocompatibility, of the resulting nanostructures. S. Kralj et al., ACS Nano 14, 16951 (2020)

The amyloid beta peptide is associated with Alzheimer’s disease and it is well-known for its propensity towards aggregation into amyloid structures that are one of the hallmarks of the pathological state. The peptide can exist in various forms and is typically composed of approximately 40 amino acids. Interestingly, it is sufficient to have just two of them, and specifically two units of phenylalanine or Phe-Phe, to have a peptide with a remarkable tendency toward self-organization into amyloid-like structures. In this work, a series of Phe-Phe analogs were studied for self-assembly into nanotubes to offer new ways to design their chemical structure through a simple approach to exert control over the formation, size, and biocompatibility, of the resulting nanostructures.

It is anticipated that further progress in this research area will shed light on important questions pertinent to the physiological as opposed to the pathological role of amyloids, and on new ways to control their formation at physiological conditions. Retrieve Article Heterochirality and Halogenation Control Phe-Phe Hierarchical Assembly Kralj S., Bellotto O., Parisi E.,Garcia A. M., Iglesias D., Semeraro S., Deganutti C., D’Andrea P., Vargiu A. V., Geremia S., De Zorzi R., Marchesan S. ACS Nano 14, 16951 (2020) DOI: 10.1021/acsnano.0c06041