Geometrically Precise Building Blocks: the Self-Assembly of β-Peptides

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.

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

“…Inspired by fascinating supramolecular aggregates produced by short hybrid peptides, we paid attention to analyze the self‐assembled propensities of peptides 1 and 2 developed in organic‐aqueous mixture. Field emission scanning electron microscopic (FE‐SEM) and transmission electron microscopy (TEM) study of peptides 1 and 2 are produced remarkable morphological features (Figure and the Supporting Information S11 and S12) at ambient conditions.…”

Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers

“…exclusively of β-amino acids (Figure 1; Cheng et al, 2001;Gopalan et al, 2015) which differ from α-amino acids due to the presence of an extra methylene between the carboxyl group and α-carbon atom (Seebach and Gardiner, 2008;Torres et al, 2010). The side chains can be positioned at either the α-or β-carbon, resulting in either β 2 or β 3 -amino acids.…”

β3-tripeptides act as sticky ends to self-assemble into a bioscaffold

“…[11][12][13] These peptides possess an extra methylene group in their backbone and are commonly referred to as b-peptide foldamers. [14][15][16][17] Peptides containing acyclic b 3 -amino acids form a unique 14-helical structure that is not adopted by a-peptides, which, in combination with N-terminal acetylation, creates a self-assembly motif. The 14-helix is of particular interest as it has almost three amino acids per turn, which creates three aligned faces of the helix.…”