Molecular Docking and Interaction Profiles of p-Hydroxybenzoic Acid and Cyclohexane-1,2,3,4,5-pentol Previously Isolated from 𝘏𝘺𝘱𝘩𝘢𝘦𝘯𝘦 𝘤𝘰𝘳𝘪𝘢𝘤𝘦𝘢 Gaertn. with Human Maltase-Glucoamylase and Pancreatic α-Amylase

Inhibition of digestive enzymes involved in carbohydrate hydrolysis is a strategy for controlling postprandial hyperglycemia in type 2 diabetes. This study investigated, using molecular docking, the interactions of _p-_hydroxybenzoic acid and cyclohexane-1,2,3,4,5-pentol, isolated from _Hyphaene coriacea_ Gaertn., with human pancreatic α-amylase and maltase-glucoamylase. Miglitol and acarbose were used as reference compounds. The three-dimensional structures of the ligands and target proteins (PDB IDs: 3L4W and 1B2Y) were retrieved from PubChem and the RCSB Protein Data Bank. Molecular docking was performed using PyRx 0.8, and the resulting interactions were analyzed with Discovery Studio Visualizer v2020. For α-amylase, the docking scores of the two phytochemicals were −5.4 and −5.5 kcal/mol, respectively, compared with −18.3 kcal/mol for acarbose. For maltase-glucoamylase, the respective scores were −5.9 kcal/mol for cyclohexane-1,2,3,4,5-pentol, −5.7 kcal/mol for _p-_hydroxybenzoic acid, and −5.5 kcal/mol for miglitol. Both phytochemicals occupied the catalytic pocket and interacted with several residues in the active sites of the enzymes studied. Although their overall binding profiles differed from those of the reference inhibitors, both compounds formed contacts with several catalytic residues also involved in the binding of the reference compounds. However, the small differences in docking scores observed for maltase-glucoamylase and the unspecified stereochemical configuration of the cyclohexane-1,2,3,4,5-pentol isolated from the plant warrant cautious interpretation. These scores indicate potential structural binding patterns but do not establish higher binding affinity or actual enzyme inhibition. Further _in vitro_ studies are therefore required to determine whether these compounds exhibit inhibitory activity, before proceeding to any subsequent _in vivo_ evaluation.