@article{MTMT:30609637,
	title = {A catalytic protein-proteomimetic complex: using aromatic oligoamide foldamers as activators of RNase S.},
	url = {https://m2.mtmt.hu/api/publication/30609637},
	author = {Hegedüs, Zsófia and Grison, Claire M. and Miles, Jennifer A. and Rodriguez-Marin, Silvia and Warriner, Stuart L. and Webb, Michael E. and Wilson, Andrew J.},
	doi = {10.1039/c9sc00374f},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {10},
	unique-id = {30609637},
	issn = {2041-6520},
	abstract = {Foldamers are abiotic mols. that mimic the ability of bio-macromols. 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 mol. recognition of diverse and complex targets. Far less explored is whether this mimicry of nature can extend to more advanced functions of biol. macromols. 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. [on SciFinder(R)]},
	year = {2019},
	eissn = {2041-6539},
	pages = {3956-3962},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167}
}