Issue 14, 2019

A catalytic protein–proteomimetic complex: using aromatic oligoamide foldamers as activators of RNase S

Abstract

Foldamers are abiotic molecules that mimic the ability of bio-macromolecules to adopt well-defined and organised secondary, tertiary or quaternary structure. Such templates have enabled the generation of defined architectures which present structurally defined surfaces that can achieve molecular recognition of diverse and complex targets. Far less explored is whether this mimicry of nature can extend to more advanced functions of biological macromolecules such as the generation and activation of catalytic function. In this work, we adopt a novel replacement strategy whereby a segment of protein structure (the S-peptide from RNase S) is replaced by a foldamer that mimics an α-helix. The resultant prosthetic replacement forms a non-covalent complex with the S-protein leading to restoration of catalytic function, despite the absence of a key catalytic residue. Thus this functional protein–proteomimetic complex provides proof that significant segments of protein can be replaced with non-natural building blocks that may, in turn, confer advantageous properties.

Graphical abstract: A catalytic protein–proteomimetic complex: using aromatic oligoamide foldamers as activators of RNase S

Supplementary files

Article information

Article type
Edge Article
Submitted
22 1月 2019
Accepted
21 2月 2019
First published
21 2月 2019
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2019,10, 3956-3962

A catalytic protein–proteomimetic complex: using aromatic oligoamide foldamers as activators of RNase S

Z. Hegedus, C. M. Grison, J. A. Miles, S. Rodriguez-Marin, S. L. Warriner, M. E. Webb and A. J. Wilson, Chem. Sci., 2019, 10, 3956 DOI: 10.1039/C9SC00374F

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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