Mark P Del Borgo, Ketav Kulkarni and Marie-Isabel Aguilar Pages 3772 - 3785 ( 14 )
β-Amino acids are being increasingly used in the design of bioactive ligands and more recently in the generation of novel biomaterials. Peptides containing either individual β-amino acid substitutions or peptides comprised entirely of β-amino acids, display unique properties in terms of their structural and/or chemical characteristics. β-Peptides form well-defined secondary structures that exhibit different geometries compared to the corresponding α-peptides. β-Peptides, including α-peptides containing only one or two β-amino acids, can be easily modified with different functional groups and are metabolically stable and, together with the predictable side chain topography, have led to the design of a growing number of bioactive β-peptides with a range of biological targets and therapeutic applications. More recently, our understanding of the folding and self-assembly of β-peptides has resulted in the generation of novel biomaterials. The focus of this review is to examine how the structural and chemical properties of β-peptides have been exploited in the design of bioactive peptides and selfassembled nanomaterials.
β-Peptides, β-amino acids, peptidomimetic, bioactive ligand, proteolytic stability, self-assembly, biomaterials.
Department of Biochemistry & Molecular Biology, Monash University Clayton, VIC, 3800, Melbourne, Victoria, Department of Biochemistry & Molecular Biology, Monash University Clayton, VIC, 3800, Melbourne, Victoria, Biomedicine Discovery Institute & Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, Vic. 3800