Pathogenesis of Alzheimer’s is mainly preceded by aggregation of β-amyloids (Aβ). Beta-site amyloid precursor protein Cleaving Enzyme-1 (BACE-1) is a rate-limiting enzyme in the production of Aβ. DFT calculations based on deduced from time dependent self-consistent field method show that 3-Aminopropane-1-sulfonic acid (3-APS) has a tendency for polar interactions and reactivity in binding pocket of BACE-1 based on the energies of the highest occupied and the lowest unoccupied molecular orbitals. Energy gap of frontier molecular orbitals was calculated to be 3.8523 eV reasonably describing global reactivity descriptors. Molecular electrostatic potential and Mulliken population charge analysis show electronegative behaviour and nucleophilic dominance of 3-APS. Drug-likeness predictions exposed the best agreement to Lipinski’s rule of five and ADMET properties. Post-docking results analysis indicates that, most stable binding pose of ligand with no root mean square deviation has the binding affinity of -3.6 kcal/mol. Least stable conformation shows an affinity of -3.2 kcal/mol. Conventional hydrogen bonds were found to be dominant interactions where the participating residues were aspartic acid (ASP) and glycine (GLY) of chain A of BACE-1. Hydrogen bonding between amino group of ligand and GLY of receptor site recorded the longest distance of 2.5128 Å. Maximum dihedral angle of 158.485° was observed in between sulfonyl group of ligand and ASP. This is attributed to steric effect around sulfonyl group within pocket. Calculated DFT parameters and docking interactions could share with varying degree to significantly affect the binding affinity of 3-APS with BACE-1 receptor.