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Biological Applications of Foldamers

“…The strategy is most likely to be productive if the mere presence of the bioactive functionalities is sufficient to exert bioactivity (which is rare), or if the foldamer scaffold inherently presents the bioactive functionalities with a similar spatial arrangement compared to the natural biopolymer and the backbone is not directly involved in binding. For example, somatostatin receptor binding b-peptides adopt a turn structure similar to the natural a-peptide somatostatin [149][150][151]. However, biologically active molecules often present functionalities in orientations significantly different from foldamer scaffolds, and therefore more sophisticated design strategies are necessary.…”

“…8.8). Initially, cyclic b-peptide tetramers were employed to present the side chains of the key residues of somatostatin Phe-Trp-Lys-Thr [149,150]. Computational modeling showed that the constraints imposed by the cyclic structure matched reasonably well with the type II 0 b-turn of a-peptides.…”

Investigation of racemisation in peptide synthesis within a micro reactor

“…In addition, b-peptides have attracted much interest due to their structural 11,12 and biological properties. 13 In particular, their stability to degradation by peptidases 14,15 makes them potentially superior to the drugs derived from a-amino acids. However, many peptides also contain a-amino acid residues which are prone to racemisation.…”

Preparation ofβ2-Homotryptophan Derivatives forβ-Peptide Synthesis

“…With b-peptides carrying tryptophan side chains, we have the means of mimicking yet other a-peptidic activities. Whereas the HÀb 3 -HTrpÀOH is available by Arndt-Eistert homologation of the natural tryptophan [29], the b 2 -analog has not been described 1 ); on the other hand, b 2 -amino acid residues are especially important for the construction of turns [22] and of 12/10 helices [21]. The preparation of b 2 -HTrp derivatives in either enantiomeric form is described herein.…”