Cyclin-dependent kinase 6 (CDK6) is linked with a
cyclin partner and plays a crucial role in the early stages of
cancer development. It is currently a potential
drug target for developing therapeutic molecules targeting
cancer therapy. Here, we have identified
taurine as an inhibitor of CDK6 using combined in silico and experimental studies. We performed various experiments to find the binding affinity of
taurine with CDK6. Molecular docking analysis revealed critical residues of CDK6 that are involved in
taurine binding. Fluorescence measurement studies showed that
taurine binds to CDK6 with a significant binding affinity, with a binding constant of K = 0.7 × 107 M-1 for the CDK6-taurine complex.
Enzyme inhibition assay suggested
taurine as a good inhibitor of CDK6 possessing an IC50 value of 4.44 μM. Isothermal titration calorimetry analysis further confirmed a spontaneous binding of
taurine with CDK6 and delineated the thermodynamic parameters for the CDK6-taurine system. Altogether, this study established
taurine as a CDK6 inhibitor, providing a base for using
taurine and its derivatives in CDK6-associated
cancer and other diseases.