The University of Southampton
University of Southampton Institutional Repository

A Modular Synthesis of Conformationally Preorganised Extended β-Strand Peptidomimetics

A Modular Synthesis of Conformationally Preorganised Extended β-Strand Peptidomimetics
A Modular Synthesis of Conformationally Preorganised Extended β-Strand Peptidomimetics

A promising strategy for mediating protein–protein interactions is the use of non-peptidic mimics of secondary structural protein elements, such as the α-helix. Recent work has expanded the scope of this approach by providing proof-of-principle scaffolds that are conformationally biased to mimic the projection of side-chains from one face of another common secondary structural element—the β-strand. Herein, we present a synthetic route that has key advantages over previous work: monomers bearing an amino acid side-chain were pre-formed before rapid assembly to peptidomimetics through a modular, iterative strategy. The resultant oligomers of alternating pyridyl and six-membered cyclic ureas accurately reproduce a recognition domain of several amino acid residues of a β-strand, demonstrated herein by mimicry of the i, i+2, i+4 and i+6 residues.
0947-6539
14699-14702
Yamashita, Tohru
1fb50b71-f393-48b4-8707-27cbb7a22958
Knipe, Peter C.
a75b6ed7-4d9b-45fc-aacc-49e9e0d0b266
Busschaert, Nathalie
bf307f09-0a86-4a03-afd8-4b0a59a8f72b
Thompson, Sam
99b7e34e-fe24-401c-b7b0-64e56cbbbcb1
Hamilton, Andrew D.
048a6c75-91bf-4555-ab12-ce885eee65dd
Yamashita, Tohru
1fb50b71-f393-48b4-8707-27cbb7a22958
Knipe, Peter C.
a75b6ed7-4d9b-45fc-aacc-49e9e0d0b266
Busschaert, Nathalie
bf307f09-0a86-4a03-afd8-4b0a59a8f72b
Thompson, Sam
99b7e34e-fe24-401c-b7b0-64e56cbbbcb1
Hamilton, Andrew D.
048a6c75-91bf-4555-ab12-ce885eee65dd

Yamashita, Tohru, Knipe, Peter C., Busschaert, Nathalie, Thompson, Sam and Hamilton, Andrew D. (2015) A Modular Synthesis of Conformationally Preorganised Extended β-Strand Peptidomimetics. Chemistry - A European Journal, 21 (42), 14699-14702. (doi:10.1002/chem.201501366).

Record type: Article

Abstract


A promising strategy for mediating protein–protein interactions is the use of non-peptidic mimics of secondary structural protein elements, such as the α-helix. Recent work has expanded the scope of this approach by providing proof-of-principle scaffolds that are conformationally biased to mimic the projection of side-chains from one face of another common secondary structural element—the β-strand. Herein, we present a synthetic route that has key advantages over previous work: monomers bearing an amino acid side-chain were pre-formed before rapid assembly to peptidomimetics through a modular, iterative strategy. The resultant oligomers of alternating pyridyl and six-membered cyclic ureas accurately reproduce a recognition domain of several amino acid residues of a β-strand, demonstrated herein by mimicry of the i, i+2, i+4 and i+6 residues.

Text
cej 2015 14,699.pdf - Version of Record
Restricted to Repository staff only
Request a copy

More information

Published date: 17 August 2015
Organisations: Chemistry

Identifiers

Local EPrints ID: 403569
URI: http://eprints.soton.ac.uk/id/eprint/403569
ISSN: 0947-6539
PURE UUID: 5008983b-33cd-4386-af49-e4a6e1948349
ORCID for Sam Thompson: ORCID iD orcid.org/0000-0001-6267-5693

Catalogue record

Date deposited: 06 Dec 2016 11:23
Last modified: 05 Nov 2019 01:33

Export record

Altmetrics

Contributors

Author: Tohru Yamashita
Author: Peter C. Knipe
Author: Nathalie Busschaert
Author: Sam Thompson ORCID iD
Author: Andrew D. Hamilton

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×