CREB Binding Protein (CBP) Inhibitors

CREB Binding Protein (CBP) inhibitors represent a category of molecules that modulate the activity of the CREB Binding Protein, a critically important transcriptional coactivator in various cellular processes. CBP, along with its close paralog p300, operates at the center of a myriad of signaling pathways by bridging the DNA-bound transcription factors and the basic transcriptional machinery. This function is achieved through its histone acetyltransferase (HAT) activity, which modulates the chromatin structure and makes DNA more accessible for transcription. CBP/p300, through this enzymatic activity, acetylates lysine residues on histones, which serves as a mark for active transcription and impacts gene expression. Due to its pivotal role in transcriptional regulation, CBP has emerged as a key player in various physiological and cellular mechanisms. CBP inhibitors predominantly target the HAT activity of CBP. By inhibiting this enzymatic function, these molecules can effectively modulate the acetylation status of histones and consequently the transcriptional output. The specificity of CBP inhibitors varies, with some compounds targeting both CBP and p300, while others show selectivity for one over the other. The design and study of these inhibitors have illuminated critical aspects of CBP function, including its interactions with other proteins and its role in gene expression dynamics. These insights into the molecular workings of CBP not only deepen our understanding of transcriptional regulation but also open avenues for exploring the intricate interplay of CBP in various cellular contexts.