[2] Balanol was discovered in 1993 in the search for novel inhibitors of PKC, a member of a family of serine/threonine kinases whose overactivation is associated with numerous human diseases of signal transduction including cancer.

[3] Indeed, balanol, its chemically altered analogs, and their interactions with PKA in particular are used to illuminate the roles of selectivity and protein flexibility in the inhibition of kinases.

For instance, the X-ray crystal structure of balanol in complex with PKA was used in order to confer selectivity and to improve pharmacological efficacy of inhibitors of the H. sapiens Akt (PKB), another serine/threonine protein kinase implicated in the proper functioning of many cellular processes.

For example, modifications of the benzophenone rings, analogs of the phosphate groups of ATP, produce unusually potent and specific protein kinase inhibitors.

Elimination of the hydroxyl group from the benzophenone ring (producing 10"-deoxybalanol), for instance, elicits selectivity two orders of magnitude greater for PKA over PKC.

[1] Balanol prevents functioning by binding competitively to the catalytic domain of PKC and PKA with an affinity (Ki ≥ 4 nM) three orders of magnitude greater than for ATP.

[5] The adenine subsite of PKA has hydrophobic components and has the potential to donate and accept electrons to make hydrogen bonds with one or two planar cyclic rings.

Specifically, the backbone nitrogen of Val123 and the carbonyl oxygen atom of Glu121 can form hydrogen bonds with balanol's single hydroxyl group of the 4-hydroxyl benzoyl moiety.

Mimetics of ATP like balanol can be anchored within the hydrophobic adenine-binding pocket because their planar substituents can make favorable nonpolar interactions.

[6] Balanol exhibits the most potent inhibitory effect (Ki = 1.6–6.4  nM) on cGMP-dependent protein kinase (PKG), PKA, and PKC, including isoforms.