Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 21st October 2020 from 07:00 AM to 07:00 PM (BST).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 12, 2014
Previous Article Next Article

Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

Author affiliations

Abstract

The ability of various functional groups to engage the acetyl-lysine (KAc) binding site within bromo- and extra-terminal domain (BET) protein family members BRD2, BRD3 and BRD4 was evaluated by screening small molecular fragments – coupled to a known arylsulfonamide scaffold – in biochemical inhibition assays. Useful structure activity relationships have been established and novel functional groups that bind to the KAc binding pocket identified. Additional microsomal degradation studies were also undertaken revealing significant differences in metabolic stability between two commonly employed BET inhibitor fragments.

Graphical abstract: Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

Back to tab navigation

Supplementary files

Article information


Submitted
23 Apr 2014
Accepted
20 Jun 2014
First published
23 Jun 2014

Med. Chem. Commun., 2014,5, 1834-1842
Article type
Concise Article

Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

P. P. Sharp, J. Garnier, D. C. S. Huang and C. J. Burns, Med. Chem. Commun., 2014, 5, 1834
DOI: 10.1039/C4MD00182F

Search articles by author

Spotlight

Advertisements