Casein Kinase 2 (CK2) is an ubiquitous hetrotetrameric eukaryotic serine/threonine protein kinase. CK2 has important roles in different cellular functions. This enzyme enhances cancer phenotype by blocking apoptosis and stimulating cell growth. Thus, inhibition of CK2 can induce the physiological process of apoptosis leading to tumor cell death. Large number of compounds has been developed as kinase inhibitors including CK2 inhibitors. Most of the CK2 inhibitors contain a heterocyclic backbone which fits into the active site of the CK2α subunit and competes with the ATP. Recently we reported on the development of compound 3: di 2,6-Di(furan-3-yl)anthracen-9,10-dion as an active CK2 inhibitor.

With the aim of finding new inhibitors for this target a series of di-substituted 9,10- Dihydrophenanthrene was designed as CK2 inhibitors and docked in crystal structure of the enzyme to evaluate their ability to fit in the active site. The main idea was to explore if the 9,10-Dihydrophenanthrene backbone is more suitable for binding than the backbone of compound 3 and to determine if the introduced functional groups can form hydrogen bonds with the amino acid residue. Some of the designed compounds were synthesized and tested in vitro as well.