investigation of the interaction of some alkaloids derived from marine algae’s with human acetylcholinesterase: in silico study

Introduction: nowadays, acetylcholinesterase inhibitors are commonly used to improve the symptoms of alzheimer's disease and central nervous system disorders. marine algae’s contain compounds like alkaloids that have many biological activities. we aimed to investigate the inhibitory effects of some alkaloids with human acetylcholinesterase using molecular docking.materials and methods: in this study, the interaction of 19 alkaloid compounds with human acetylcholinesterase (hache) was investigated using molecular docking. the initial structure of the compounds was optimized using mm2 method by chem3d software; the compounds were evaluated as inhibitors on the gap of the active site of the enzyme by autodackvina software, and the output results were analyzed by discovery studio software.results: the results showed that most of these compounds act as inhibitors with good binding energy (-7.7 to -9.8 kcal/mol). the best performance is related to the three compounds including caulerpin, martefragin a and n-acetyl tyramine. caulerpin was involved in hydrogen bonding with an affinity of -9.6 with the amino acids histidine: 405, arginine: 296, and asparagine: 233. martefragin a was involved in hydrogen bonding with an affinity of -9.6 with the amino acids serine: 293, phenylalanine: 295, and arginine: 296, respectively. n-acetyl tyramine was involved in hydrogen bonding with an affinity of -9.8 with the amino acids asparagine: 186, lysine: 53, and glycine: 14.conclusion: the results of this study suggest that most of these alkaloid compounds can inhibit this enzyme by binding to the cleavage site of the active site of hache, and thus are suitable options for further studies to design new anticholinesterase drugs.