Tools
Tools
Howell, Lesley Ann and Beekman, Andrew Michael 
ORCID: https://orcid.org/0000-0002-3056-6406
(2021)
In silico peptide-directed ligand design complements experimental peptide-directed binding for protein–protein interaction modulator discovery.
RSC Chemical Biology, 2 (1).
pp. 215-219.
ISSN 2633-0679
Preview |
PDF (Published_Version)
- Published Version
Available under License Creative Commons Attribution Non-commercial. Download (2MB) | Preview |
Abstract
Using the protein–protein interaction of Mcl-1/Noxa, two methods for efficient modulator discovery are directly compared. In silico peptide-directed ligand design is evaluated against experimental peptide-directed binding, allowing for the discovery of two new inhibitors of Mcl-1/Noxa with cellular activity. In silico peptide-directed ligand design demonstrates an in vitro hit rate of 80% (IC50 < 100 μM). The two rapid and efficient methods demonstrate complementary features for protein–protein interaction modulator discovery.
| Item Type: | Article |
|---|---|
| Additional Information: | Funding Information: This work was funded in part through a Royal Society Research Grant RGS/R1/201008 and EPSRC New Investigator Grant EP/ M006379/1. We acknowledge the EPSRC UK National Mass Spectrometry Facility at Swansea University. |
| Uncontrolled Keywords: | biochemistry,molecular biology,biochemistry, genetics and molecular biology (miscellaneous),chemistry (miscellaneous) ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Pharmacy (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Chemical Biology and Medicinal Chemistry (former - to 2021) |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 20 Nov 2020 00:53 |
| Last Modified: | 23 Oct 2024 23:55 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/77738 |
| DOI: | 10.1039/D0CB00148A |
Downloads
Downloads per month over past year
Actions (login required)
 |
View Item |