As one of the most important families of non-natural polymers with the propensity
to form well-defined secondary structures, the beta-peptides are attracting increasing
attention. The compounds incorporating beta-amino acid residues have found various
applications in medicinal chemistry and biochemistry. The conformational pool of beta-peptides
comprises several periodic folded conformations, which can be classified as helices,
and nonpolar and polar strands. The latter two are prone to form pleated sheets. The
numerous studies that have been performed on the side-chain dependence of the stability
of the folded structures allow certain conclusions concerning the principles of design
of the beta-peptide foldamers. The folding propensity is influenced by local torsional,
side-chain to backbone and long-range side-chain interactions. Although beta-peptide
foldamers are sensitive to solvent, the systematic choice of the side-chain pattern
and spatiality allows the design of the desired specific secondary structure. The
application of beta-peptide foldamers may open up new directions in the synthesis
of highly organized artificial tertiary structures with biochemical functions.
