Geometrically precise building blocks: the self-assembly of beta-peptides

Romila D Gopalan, Mark P Del Borgo, Adam I Mechler, Patrick Perlmutter, Marie-Isabel Isabel Aguilar

Research output: Contribution to journalArticleResearchpeer-review

35 Citations (Scopus)

Abstract

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 this mini-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.
Original languageEnglish
Pages (from-to)1417 - 1423
Number of pages7
JournalChemistry and Biology
Volume22
Issue number11
DOIs
Publication statusPublished - 2015

Cite this