A Selenylation-Isocyanation-Amine Addition Strategy Targeting Prenylated Derivatives to Disrupt Oncogenic Rat Sarcoma Level.

Abstract

In recent years, significant strides have been made in protein prenylation research, a critical post-translational modification essential for modulating cellular signaling. Central to this advancement is the selenylation-isocyanation-amine Addition strategy, which employs amine-functionalized fluorescent or biotin-tagged probes to selectively label or isolate prenylated molecules. Herein, Rat Sarcoma (RAS) protein regulation in HCT116 cell lines through the development of a novel prenylation labeling method is investigated. This approach provides insights into the functional dynamics of prenylated proteins and enables targeted manipulation of these molecules. While this work primarily establishes a methodological advance, it lays the foundation for future studies to elucidate RAS-related oncogenic signaling pathways and explore therapeutic strategies targeting prenylation-dependent processes.