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α,β 2,3 -Disteroisomeric foldamers of general formula Boc( S- Ala-β-2 R ,3 R- Fpg) n OMe or Boc( S- Ala-β-2 S ,3 S- Fpg) n OMe were prepared from both enantiomers of  syn  H-2-(2-F-Phe)-h-PheGly-OH (named β-Fpg) and  S- alanine. Our peptides show two appealing features for biomedical applications: the presence of fluorine, attractive for non-covalent interactions, and aryl groups, crucial for π-stacking. A conformational study was performed, using IR, NMR and computational studies of diastereoisomeric tetra- and hexapeptides containing the β 2,3 -amino acid in the  R,R - and  S,S -stereochemistry, respectively. We found that the stability of peptide conformation is dependent on the stereochemistry of the β-amino acid. Combining  S -Ala with β-2 R,3R -Fpg, a stable extended β-strand conformation was obtained. Furthermore, β-2 R,3R -Fpg containing hexapeptide self-assembles to form antiparallel β-sheet structure stabilized by intermolecular H-bonds and π,π-interactions. These features make peptides containing the β 2,3 -fluoro amino acid very appealing for the development of bioactive proteolytically stable foldameric β-sheets as modulators of protein-protein interaction (PPI).

Fluoro-Aryl Substituted α,β2,3-Peptides in the Development of Foldameric Antiparallel β-Sheets: A Conformational Study