Jump to main content
Jump to site search

Issue 12, 2020
Previous Article Next Article

A modular approach for organizing dimeric coiled coils on peptoid oligomer scaffolds

Author affiliations

Abstract

We report a general approach to promote the folding of synthetic oligopeptides capable of forming homodimeric coiled coil assemblies. By pre-organizing the peptides on macrocyclic oligomer scaffolds, the stability of the coiled coils is enhanced with an observed increase in the melting temperature of 30 °C to 40 °C. Molecular dynamics simulations substantiate the hypothesis that the enhanced stability is established by constraining motion at the peptide termini and by pre-organizing intramolecular helix–helix contacts. We demonstrate the modularity of this approach by using a family of peptoid scaffolds to promote the folding of a dimeric coiled coil. Importantly, this strategy for templating coiled coils allows preservation of native amino acid sequences. Comparing a macrocyclic peptoid scaffold to its linear counterparts indicates that both types of assemblies are effective for organizing stable coiled coils. These results will guide future designs of coiled coil peptides for biomedical applications and as building blocks for more complex supramolecular assemblies.

Graphical abstract: A modular approach for organizing dimeric coiled coils on peptoid oligomer scaffolds

Back to tab navigation

Supplementary files

Article information


Submitted
21 Dec 2019
Accepted
03 Mar 2020
First published
09 Mar 2020

Org. Biomol. Chem., 2020,18, 2312-2320
Article type
Paper

A modular approach for organizing dimeric coiled coils on peptoid oligomer scaffolds

L. Jiang and K. Kirshenbaum, Org. Biomol. Chem., 2020, 18, 2312
DOI: 10.1039/D0OB00453G

Social activity

Search articles by author

Spotlight

Advertisements