Identification of new leads against ubiquitin specific protease-7 (USP7): a step towards the potential treatment of cancers.

ABSTRACT: Ubiquitin-specific protease-7 (USP7) is an important drug target as it regulates multiple proteins and genes (such as MDM2 and p53) with roles in cancer progression. Its inhibition can hinder the function of oncogenes, increase tumor suppression, and enhance immune response. The current study was designed to express USP7 in a prokaryotic system, followed by screening of small molecules against it using biophysical methods, primarily STD-NMR technique. Among them, 12 compounds showed interaction with USP7 as inferred from NMR-based screening. These compounds further caused destabilization of USP7 by reducing its melting temperature (T _m) up to 6 °C in thermal shift assay. Molecular docking and simulation studies revealed that these compounds bind to the putative substrate

SUBMITTER: Javaid S 

PROVIDER: S-EPMC11492238 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature