Citation

BibTex format

@article{Barnard:2015:10.1002/anie.201410810,
author = {Barnard, A and Long, K and Martin, HL and Miles, JA and Edwards, TA and Tomlinson, DC and Macdonald, A and Wilson, AJ},
doi = {10.1002/anie.201410810},
journal = {Angewandte Chemie - International Edition},
pages = {2960--2965},
title = {Selective and potent proteomimetic inhibitors of intracellular protein–protein interactions},
url = {http://dx.doi.org/10.1002/anie.201410810},
volume = {54},
year = {2015}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Inhibition of protein–protein interactions (PPIs) represents a major challenge in chemical biology and drug discovery. α-Helix mediated PPIs may be amenable to modulation using generic chemotypes, termed “proteomimetics”, which can be assembled in a modular manner to reproduce the vectoral presentation of key side chains found on a helical motif from one partner within the PPI. In this work, it is demonstrated that by using a library of N-alkylated aromatic oligoamide helix mimetics, potent helix mimetics which reproduce their biophysical binding selectivity in a cellular context can be identified.
AU - Barnard,A
AU - Long,K
AU - Martin,HL
AU - Miles,JA
AU - Edwards,TA
AU - Tomlinson,DC
AU - Macdonald,A
AU - Wilson,AJ
DO - 10.1002/anie.201410810
EP - 2965
PY - 2015///
SN - 1433-7851
SP - 2960
TI - Selective and potent proteomimetic inhibitors of intracellular protein–protein interactions
T2 - Angewandte Chemie - International Edition
UR - http://dx.doi.org/10.1002/anie.201410810
UR - https://onlinelibrary.wiley.com/doi/full/10.1002/anie.201410810
UR - http://hdl.handle.net/10044/1/32307
VL - 54
ER -