Labdane diterpenoids are phytochemicals which have been reported effectively against acetylcholinesterase inhibition. Butyrylcholinesterase is another enzyme involved in hydrolysis of acetylcholine in the brain. Both enzymes are regarded as important therapeutic target for Alzheimer’s disease. Nonetheless, study on the effect of labdane diterpenoids towards butyrylcholinesterase inhibition is scarce. This project aimed to study the pharmacokinetic profiles of labdane diterpenoids of Alpinia genus via in silico methods and to evaluate their binding interactions in the active site of butyrylcholinesterase through molecular docking. A series of thirty labdane diterpenoids from Alpinia genus were investigated for their physicochemical properties using Molinspiration server and the pharmacokinetics profiles using pkCSM. Docking systems consisting of butyrylcholinesterase protein (PDB ID: 4BDS) and labdane diterpenoids were subjected to docking studies using AutoDockTools. Protein-Ligand Interaction Profiler was used to analyse the docking outputs; LigPlot Plus was used to illustrate the binding interactions between butyrylcholinesterase protein and labdane diterpenoids. A total of twenty labdane diterpenoids met the requirement of Lipinski’s rule and complied to Veber rule. Several labdane diterpenoids in the present study have exhibited drug likeness, good oral bioavailability as well as considerable drug distribution and blood-brain-barrier penetration based on in silico prediction. All compounds were shown to have relatively good binding within the binding site of butyrylcholinesterase from the docking studies in comparison to the co-crystallised ligand, tacrine based on the binding energy; their binding energies ranged from -17.70 kcal/mol to -7.3 kcal/mol versus that of tacrine with binding energy of -7.71 kcal/mol. Hydrogen bonding and hydrophobic interactions were found as the main binding interactions between the binding site residues and labdane diterpenoids. Amongst the compounds, ligand no. 1 showed the highest binding energy of -16.00 kcal/mol and the lowest estimated Ki of 1.86 pM. In conclusion, several labdane diterpenoids in the present study have demonstrated good pharmacokinetic profiles based on the in silico prediction. These compounds were also shown to have relatively good binding within the binding site of butyrylcholinesterase based on the molecular docking studies. Keywords: Labdane diterpenoids, butyrylcholinesterase, Alzheimer’s disease, pharmacokinetics, molecular docking