Exploring structural and biological insights of TEAD through rational design and synthesis of niflumic acid derivatives

J Enzyme Inhib Med Chem. 2024 Dec;39(1):2419925. doi: 10.1080/14756366.2024.2419925. Epub 2024 Nov 4.

Abstract

Transcriptional enhanced associate domain (TEAD) transcription factors undergo auto-palmitoylation, which is critical to mediate their function and maintain stability. Targeting the palmitate binding pocket of TEAD holds considerable promise for drug discovery, and it can be characterised into three components: a conserved cysteine, a hydrophobic main pocket, and a hydrophilic side pocket. Endogenous palmitate and several known TEAD inhibitors interact with the cysteine and hydrophobic residues in the deep hydrophobic pocket. We anticipate that precise targeting of the polar side pocket could facilitate the discovery of inhibitors with enhanced potencies and properties. Herein, we selected niflumic acid as the core scaffold suitable for targeting the three characteristic components of TEAD palmitate pocket. Reversible and irreversible compounds with substituents capable of directing each part of the palmitate pocket were designed. The newly synthesised compounds inhibited the palmitoylation and transcriptional activity of TEAD and elicited growth-inhibitory effects against several carcinomas, including mesothelioma.

Keywords: Hippo pathway; TEAD inhibitor; mesothelioma; palmitate pocket; rational design.

MeSH terms

  • Antineoplastic Agents* / chemical synthesis
  • Antineoplastic Agents* / chemistry
  • Antineoplastic Agents* / pharmacology
  • Cell Line, Tumor
  • Cell Proliferation* / drug effects
  • DNA-Binding Proteins / antagonists & inhibitors
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Dose-Response Relationship, Drug*
  • Drug Design*
  • Drug Screening Assays, Antitumor*
  • Humans
  • Molecular Structure
  • Niflumic Acid* / chemical synthesis
  • Niflumic Acid* / chemistry
  • Niflumic Acid* / pharmacology
  • Structure-Activity Relationship
  • TEA Domain Transcription Factors
  • Transcription Factors* / antagonists & inhibitors
  • Transcription Factors* / metabolism

Substances

  • Niflumic Acid
  • Antineoplastic Agents
  • Transcription Factors
  • TEA Domain Transcription Factors
  • DNA-Binding Proteins

Grants and funding

This research was supported by the National Research Foundation of Korea (NRF), funded by the Korea government (MSIT) (No. 2021R1A2C1003358), and by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2020R1I1A1A01072516). Additionally, the current research was supported by the National Research Foundation of Korea (NRF) and the Commercialisation Promotion Agency for R&D Outcomes, funded by the Korea government (MSIT) (No. RS-2023–00233462).