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

Gopalan, Romila D. and Del Borgo, M.P. and Mechler, Adam and Perlmutter, P. and Aguilar, M.I. (2015) Geometrically Precise Building Blocks: the Self-Assembly of beta-Peptides. Chemistry & Biology , 22 . pp. 1417-1423. ISSN 1074-5521

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    Abstract

    Peptides comprised entirely of b-amino acids, or b-peptides, have attracted substantial interest over the past 25 years due to their unique structural and chemical characteristics. b-Peptides form well-defined secondary structures that exhibit different geometries compared with their a-peptide counterparts, giving rise to their foldamer classification. b-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 b-peptides with a range of biological targets. The strategic engineering of chemical and topographic properties has also led to the design of b-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 b-peptide assemblies have been exploited in the design of self-assembled proteomimetic bundles and nanomaterials.

    Item Type: Journal Article
    Subjects: Q Science > QD Chemistry
    R Medicine > RM Therapeutics. Pharmacology
    Divisions: Faculty of Science, Technology and Environment (FSTE) > School of Biological and Chemical Sciences
    Depositing User: Dr Romila Devi Gopalan
    Date Deposited: 02 Dec 2015 15:09
    Last Modified: 02 Dec 2015 15:09
    URI: http://repository.usp.ac.fj/id/eprint/8614
    UNSPECIFIED

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