Structural and functional insights into an anticancer peptide candidate derived from the EP400NL C-terminal domain

EP400 N-terminal Like (EP400NL) is a recently characterized transcriptional coactivator implicated in chromatin remodeling and oncogenic signaling. Although its precise function remains incompletely understood, emerging evidence suggests that EP400NL contributes to transcriptional regulatory networks relevant to tumor progression. In this study, we investigated the structural and functional properties of the C-terminal domain (CTD) of EP400NL using bioinformatic and molecular modeling approaches and evaluated the anticancer potential of a peptide derived from this region. Molecular dynamics simulations indicated that the CTD forms an extended, flexible tail that may serve as a functional motif mediating protein-protein interactions. Cell-based assays demonstrated that delivery of the EP400NL CTD peptide or shRNA-mediated targeting of the corresponding RNA region suppresses cancer cell proliferation and clonogenicity, supporting a potential inhibitory role of this domain in tumor growth and survival. Collectively, these findings identify the EP400NL CTD as a promising structural motif for anticancer peptide development.