Structural Properties of Phenylalanine-Based Dimers Revealed Using IR Action Spectroscopy

• Main Authors: Bakels, S. (Author), Rijs, A.M (Author), Stroganova, I. (Author)
• Format: Article
• Language: English
• Published: NLM (Medline) 2022
• Subjects: chemistry; human; Humans; infrared spectroscopy; molecular beam; nanomaterial; Nanostructures; peptide; peptide aggregates; Peptides; phenylalanine; Phenylalanine; self-assembly; spectroscopy; Spectrum Analysis
• Online Access: View Fulltext in Publisher

 Peptide segments with phenylalanine residues are commonly found in proteins that are related to neurodegenerative diseases. However, the self-assembly of phenylalanine-based peptides can be also functional. Peptides containing phenylalanine residues with different side caps, composition, and chemical alteration can form different types of nanostructures that find many applications in technology and medicine. Various studies have been performed in order to explain the remarkable stability of the resulting nanostructures. Here, we study the early stages of self-assembly of two phenylalanine derived peptides in the gas phase using IR action spectroscopy. Our focus lies on the identification of the key intra- and intermolecular interactions that govern the formation of the dimers. The far-IR region allowed us to distinguish between structural families and to assign the 2-(2-amino-2-phenylacetamido)-2-phenylacetic acid (PhgPhg) dimer to a very symmetric structure with two intermolecular hydrogen bonds and its aromatic rings folded away from the backbone. By comparison with the phenylalanine-based peptide cyclic L-phenylalanyl-L-phenylalanine (cyclo-FF), we found that the linear FF dimer likely adopts a less ordered structure. However, when one more phenylalanine residue is added (FFF), a more structurally organized dimer is formed with several intermolecular hydrogen bonds.