Journal
CHEMISTRY & BIOLOGY
Volume 22, Issue 11, Pages 1417-1423Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2015.10.005
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Funding
- Australian Research Council [DP1093675, LP120200794]
- Australian Research Council [LP120200794, DP1093675] Funding Source: Australian Research Council
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Peptides comprised entirely of beta-amino acids, or beta-peptides, have attracted substantial interest over the past 25 years due to their unique structural and chemical characteristics. beta-Peptides form well-defined secondary structures that exhibit different geometries compared with their alpha-peptide counterparts, giving rise to their foldamer classification. beta-Peptide foldamers can be functionalized easily and are metabolically stable and, together with the predictable side-chain topography, have led to the design of a growing number of bioactive beta-peptides with a range of biological targets. The strategic engineering of chemical and topographic properties has also led to the design of beta-peptide mimics of higher-order oligomers. More recently, the ability of these peptides to self-assemble into complex structures of controlled geometries has been exploited in materials applications. The focus of thismini-review is on how the unique structural features of beta-peptide assemblies have been exploited in the design of self-assembled proteomimetic bundles and nanomaterials.
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