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

Autor:	Gopalan RD; Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC 3800, Australia., Del Borgo MP; Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC 3800, Australia., Mechler AI; Department of Chemistry, School of Molecular Science, La Trobe University, Bundoora, VIC 3083, Australia., Perlmutter P; School of Chemistry, Monash University, Clayton, VIC 3800, Australia., Aguilar MI; Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC 3800, Australia. Electronic address: mibel.aguilar@monash.edu.
Jazyk:	angličtina
Zdroj:	Chemistry & biology [Chem Biol] 2015 Nov 19; Vol. 22 (11), pp. 1417-1423. Date of Electronic Publication: 2015 Nov 12.
DOI:	10.1016/j.chembiol.2015.10.005
Abstrakt:	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. (Copyright © 2015 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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