In this section
@article{Date:2026:10.1039/d6cb00065g,
author = {Date, A and Wall, A and Kiely-Collins, H and Flack, T and Houghton, J and Lu, J and Thomas, A and Zhang, P and Wilson, A and Tate, E and Barnard, A},
doi = {10.1039/d6cb00065g},
journal = {RSC Chemical Biology},
title = {Proteome-wide target profiling of a-helix mimetics},
url = {http://dx.doi.org/10.1039/d6cb00065g},
year = {2026}
}
TY - JOUR
AB - The dysregulation of protein–protein interactions (PPIs) in disease states is well established, yet they are challenging to target, owing to the large surface area and featureless nature of protein binding interfaces. For targeting helix-mediated interactions, α-helix mimetics present a promising strategy. These are versatile small molecule scaffolds, capable of mimicking the hotspot residues on an α-helix. A wide range of such scaffolds have been reported, yet their target protein selectivity in the context of a whole proteome requires further exploration. Here, we report the affinity-based protein profiling of three structurally distinct classes of α-helix mimetics, N-substituted oligobenzamides, pyrrolopyrimidines, and oxopiperazines. This represents the first direct cross-comparison of different helix mimetic scaffolds, revealing significant differences in proteome-wide selectivity.
AU - Date,A
AU - Wall,A
AU - Kiely-Collins,H
AU - Flack,T
AU - Houghton,J
AU - Lu,J
AU - Thomas,A
AU - Zhang,P
AU - Wilson,A
AU - Tate,E
AU - Barnard,A
DO - 10.1039/d6cb00065g
PY - 2026///
SN - 2633-0679
TI - Proteome-wide target profiling of a-helix mimetics
T2 - RSC Chemical Biology
UR - http://dx.doi.org/10.1039/d6cb00065g
UR - https://pubs.rsc.org/cb/article/doi/10.1039/d6cb00065g/1284401/Proteome-wide-target-profiling-of-helix-mimetics
ER -
Dr Anna Barnard
Wellcome Trust Sir Henry Dale Fellow
Department of Chemistry
51³Ô¹ÏÍø
Wood Lane
London W12 0BZ
a.barnard@imperial.ac.uk
Tel: +44 (0)20 7594 8551