Syntheses and applications of enantiopure δ-amino acids and their precursors

Abstract

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A spirocyclic backbone accesses new conformational space in an extended, dipole-stabilized foldamer

“…Backbone heterogeneity has been achieved in various ways. For example, many mixed α-/β-/ γ-/δ-peptides [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31] and peptide-peptoid 32 systems have been reported, allowing conformational tuning of the resulting foldamers. Sanjayan pioneered mixed aliphatic-aromatic hybrid foldamers, incorporating phenols, BINOLs and benzamides alongside aliphatic amides [33][34][35] .…”

Asymmetric hydrogenation of exocyclic γ,δ-unsaturated β-ketoesters to functionalized chiral allylic alcohols via dynamic kinetic resolution

“…Chiral δ-amino acids are an important class of biomolecules used extensively as peptidomimetics and in the development of pharmaceuticals. 18 We noticed that carbocyclic δ-amino acid ester 16 is a key chiral intermediate to peptidomimetic 17 ( Scheme 7 ), which showed submicromolar activity on β-site amyloid precursor protein cleavage enzyme-1 (BACE-1). 19 However, long synthetic sequences (at least 11 steps) were required to complete the synthesis of such a δ-amino acid and its derivatives.…”

Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic**

“… [18] This shortfall is partly due to the paucity in synthetic methods towards the appropriate δ‐amino acid monomers. [19] Furthermore, these hybrid systems are of potential biological interest, because an α,δ‐dipeptide corresponds to an α‐amino acid trimer unit and has the potential to replace this in peptides and proteins. Nevertheless, with our eye on the catalytic potential we desired, we were drawn to the most stable of these δ‐amino acid heteromers—the H 13/11 system—because according to Hofmann‘s modelling, the α‐residues appear to be embedded within the helix, whilst the δ‐residues occupy the perimeter (Figure 1 ).…”