Hijacking the MDM2 E3 Ligase with novel BRD4-Targeting PROTACs in Pancreatic Cancer Cells

09 August 2024, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

The phenotypic effect induced by a Proteolysis-Targeting Chimera (PROTAC) can depend on several factors, including the E3 ligase recruited. For the discovery of a first-in-class PROTAC for a target of interest, the E3 ligases commonly hijacked remain the Von Hippel-Lindau (VHL) and Cereblon (CRBN) since potent and accessible ligands are readily available to recruit them. Mouse double minute 2 (MDM2) E3 ligase stands out because it regulates p53 levels to maintain cellular homeostasis. However, the synthesis of the most potent MDM2 ligands remains very complex. Here we report the discovery of novel MDM2-recruiting PROTACs incorporating rac-Nutlin-3 as a ligand with an easier synthetic tractability, further demonstrating its potential in this technology. The most promising degrader, PROTAC 3, showed preferential degradation of the BRD4 short isoform and c-Myc compared with MZ1, a validated VHL-based PROTAC.

Keywords

Targeted Protein Degradation
PROTACs
MDM2
HMD2
MIA PaCa-2
pancreatic cancer

Supplementary materials

Title
Description
Actions
Title
Supplementary information
Description
Additional immunoblotting experiments, experimental procedures for the synthesized compounds and for the biological assays, characterization data for the lead compound, and full scans of the blots. (PDF)
Actions

Comments

Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.