Abstract
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.
Keywords: β-Peptides, β-amino acids, peptidomimetic, bioactive ligand, proteolytic stability, self-assembly, biomaterials.
Current Pharmaceutical Design
Title:Using β-Amino Acids and β-Peptide Templates to Create Bioactive Ligands and Biomaterials
Volume: 23 Issue: 26
Author(s): Mark P Del Borgo, Ketav Kulkarni and Marie-Isabel Aguilar*
Affiliation:
- Biomedicine Discovery Institute & Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, Vic. 3800,Australia
Keywords: β-Peptides, β-amino acids, peptidomimetic, bioactive ligand, proteolytic stability, self-assembly, biomaterials.
Abstract: 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.
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Cite this article as:
Del Borgo P Mark, Kulkarni Ketav and Aguilar Marie-Isabel *, Using β-Amino Acids and β-Peptide Templates to Create Bioactive Ligands and Biomaterials, Current Pharmaceutical Design 2017; 23 (26) . https://dx.doi.org/10.2174/1381612823666170616083031
DOI https://dx.doi.org/10.2174/1381612823666170616083031 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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