The construction of bioactive peptides using β-amino acid-containing sequence patterns
is a very promising strategy to obtain analogues that exhibit properties of high interest
for medicinal chemistry applications. β-Amino acids have been shown to modulate the
conformation, dynamics, and proteolytic susceptibility of native peptides. They can
be either combined with α-amino acids by following specific patterns, which results
in backbone architectures with well-defined orientations of the side chain functional
groups, or assembled in de novo-designed bioactive β- or α,β-peptidic sequences. Such
peptides display various biological functions, including antimicrobial activity, inhibition
of protein-protein interactions, agonism/antagonism of GPCR ligands, and anti-angiogenic
activity.
