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=='''A Physical Model of Acetylcholinesterase in Complex with Acetylcholine and Fasciculin-II'''== | |||
Students: Mary Acheampong. Daviana Dueno, Bobby Glover, Alafia Henry, Randol Mata, Marisa VanBrakle. | |||
Teacher: Allison Granberry | |||
Mentors: Joel Sussman, Weissman Institule of Science, and Lars Westblade, touro College of Pharmacy. | |||
==='''Abstract'''=== | |||
Acetylcholinesterase(AChE) is essential for the hydrolysis of the neurotransmitter acetylcholine(ACh) in cholinergic synapses. Irreversible inhibition of AChE can lead to increased levels of ACh and ultimately death. Conversely, suppressed levels of ACh may lead to memory deficits associated with Alzheimer's disease. AChE has a deep(20A) and narrow(5A) gorge lined with 14 aromatic residues, with its active site at the bottom of the gorge. Initially, ACh binds to the peripheral anionic site(PAS) of AChE and is funneled down the gorge to the active site by interactions between the aromatic rings of the 14 aromatic residues and the quaternary ammonium ion of ACh. At the active site, ACh is oriented for hydrolysis by interactions between the catalytic anionic ion site and the quaternary ammonium ion of ACh. The Fasciculin-II(FAS-II)toxin, from the East African Green Mamba snake(''Dendroaspis angusticeps'') venom, inhibits AChE by binding to the top of the active-site gorge, and thus preventing ACh from entering into it. The Hostos-Lincoln Academy SMART(Students Modeling A Research Topic) team and MSOE have designed and made two physical models by three-dimensional(3D) printing technology: ''Torpedo californica''(''Tc'') AChE in complex with a modeled ACh ligand and ''Tc''AChE in complex with FAS-II. | |||
==='''Designing a Physical Model to Tell the Story of Acetylcholinesterase'''=== | ==='''Designing a Physical Model to Tell the Story of Acetylcholinesterase'''=== | ||