Acetylcholinesterase (AChE) is a primary target for Alzheimer's therapy while 
recently sodium glucose cotransporter 2 (SGLT2) has gained importance as a 
potential target for Type 2 Diabetes Mellitus (T2DM) therapy. The present study 
emphasizes the molecular interactions between a new Food and Drug Administration 
(FDA) approved antidiabetic drug 'Invokana' (chemically known as Canagliflozin) 
with AChE and SGLT2 to establish a link between the treatment of T2DM and 
Alzheimer's Disease (AD). Docking study was performed using 'Autodock4.2'. Both 
hydrophobic and π-π interactions play an important role in the correct 
positioning of Canagliflozin within SGLT2 and catalytic site (CAS) of AChE to 
permit docking. Free energy of binding (ΔG) for 'Canagliflozin-SGLT2' 
interaction and 'Canagliflozin - CAS domain of AChE' interaction were found to 
be -10.03 kcal/mol and -9.40 kcal/mol, respectively. During 
'Canagliflozin-SGLT2' interaction, Canagliflozin was found to interact with the 
most important amino acid residue Q457 of SGLT2. This residue is known for its 
interaction with glucose during reabsorption in kidney. However, 
'Canagliflozin-CAS domain of AChE' interaction revealed that out of the three 
amino acids constituting the catalytic triad (S203, H447 and E334), two amino 
acid residues (S203 and H447) interact with Canagliflozin. Hence, Invokana 
(Canagliflozin) might act as a potent dual inhibitor of AChE and SGLT2. However, 
scope still remains in the determination of the three-dimensional structure of 
SGLT2-Canagliflozin and AChE-Canagliflozin complexes by X-ray crystallography to 
validate the described data. Since the development of diabetes is associated 
with AD, the design of new AChE inhibitors based on antidiabetic drug scaffolds 
would be particularly beneficial. Moreover, the present computational study 
reveals that Invokana (Canagliflozin) is expected to form the basis of a future 
dual therapy against diabetes associated neurological disorders.