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: | Romila Devi Gopalan |
| Date Deposited: | 02 Dec 2015 02:09 |
| Last Modified: | 02 Dec 2015 02:09 |
| URI: | https://repository.usp.ac.fj/id/eprint/8614 |
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