| Literature DB >> 26584778 |
Romila D Gopalan1, Mark P Del Borgo1, Adam I Mechler2, Patrick Perlmutter3, Marie-Isabel Aguilar4.
Abstract
Peptides comprised entirely of β-amino acids, or β-peptides, have attracted substantial interest over the past 25 years due to their unique structural and chemical characteristics. β-Peptides form well-defined secondary structures that exhibit different geometries compared with their α-peptide counterparts, giving rise to their foldamer classification. β-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 β-peptides with a range of biological targets. The strategic engineering of chemical and topographic properties has also led to the design of β-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 this mini-review is on how the unique structural features of β-peptide assemblies have been exploited in the design of self-assembled proteomimetic bundles and nanomaterials.Entities:
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Year: 2015 PMID: 26584778 DOI: 10.1016/j.chembiol.2015.10.005
Source DB: PubMed Journal: Chem Biol ISSN: 1074-5521