Gopalan, Romila D. and Bergman, Y.E. and Del Borgo, M.P. and Aguilar, M.I. and Perlmutter, P. (2009) Synthesis of “stapled” 14 - helical β3 - peptides. UNSPECIFIED.
Full text not available from this repository.Abstract
To understand how folded polymers, such as proteins behave has inspired widespread interest in unnatural oligomers that are known to display similar folding patterns and are referred to as foldamers1. β3-Peptides foldamers, (oligomers of β3-amino acids) are among the most widely studied foldamers at present, and have been reported to adopt discrete and stable secondary helical structures. Of the many types of helices formed by β3-peptides, 14-helices are particularly interesting as they have almost 3 residues per helical turn (with a pitch of 5.0Å). This allows the side chains to be aligned perfectly in three faces. The residues at i/i+3 positions are not only on the same face of the helix but are also are relatively close in proximity to each other. The aim of this study was to explore synthetic strategies for the synthesis of novel β3-peptides on which further functionalisation on specific faces of the helix can be performed and used to create novel foldamer assemblies. β3-Peptides were synthesised incorporating O-allyl-β3-serines and allyl-β3-glycines at i/i+3 positions and efficiently “stapled” the allyl groups on β3-serines and β3-glycines via Ring Closing Metathesis (RCM) on a solid support. The CD and 2D NMR analysis showed that β3-peptides, “stapled” as well as “unstapled”, exhibited spectra in various solvents consistent with 14 helix signature. Thus, the “stapled” side chains on the β-peptides can now be used as a template to attach functional groups to generate new molecules of biological significance.
| Item Type: | Other |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Science, Technology and Environment (FSTE) > School of Biological and Chemical Sciences |
| Depositing User: | Romila Devi Gopalan |
| Date Deposited: | 11 Sep 2017 22:50 |
| Last Modified: | 11 Sep 2017 22:50 |
| URI: | http://repository.usp.ac.fj/id/eprint/10008 |
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