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Issue 14, 2019
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A catalytic protein–proteomimetic complex: using aromatic oligoamide foldamers as activators of RNase S

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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

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Supplementary files

Article information


Submitted
22 Jan 2019
Accepted
21 Feb 2019
First published
21 Feb 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 3956-3962
Article type
Edge Article

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

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