1Department of pharmacy, Al-Zahrawi University College, Karbala, Iraq
2College of pharmacy, University of Ahl Al-Bait, Karbala, Iraq
3Department of Pharmaceutical Sciences, Northeast Ohio Medical University, College of Pharmacy, Rootstown, Ohio, 44272, USA
*Corresponding author: Hasanain Abdulhameed Odhar, Department of pharmacy, Al-Zahrawi University College, Karbala, Iraq. Tel: 009647725300923, Email: hodhar3@gmail.com
Online published on 27 November, 2019.
Alzheimer's disease is the one of the most form of dementia that mainly affects geriatric population. It is a complex neurodegenerative disorder that is characterized by aggregation of proteinaceous deposits within affected neurons. This impacting was Associated with loss of memory and deterioration of cognition can result in disability and poor quality of life. Pathogenesis of Alzheimer's disease has caused by multifactorial and not fully understood. The available medications such as acetyl cholinesterase suppressor can't halt disease development. Current research attempts to focus toward targeting more than one pathogenic mechanism associated with Alzheimer's disease such as approach may modify sick course and minimize neurodegeneration rate. Other inhibitor is 8-hydroxyquinoline is a commonly used building block that had been utilized in the synthesis of several centrally active medications. 8-hydroxyquinoline has a well-known ability to quench free radicals and chelate metals. In this trend, our virtual analysis study indicated that combining two molecules of 8-hydroxyquinoline can produce compound 5476423. In vitro analysis recorded that compound 5476423 can inhibit acetyl cholinesterase within early micro molar range. Michaelis-Menten kinetics study revealed that compound 5476423 can decrease maximum velocity of hydrolysis reaction catalyzed by acetylcholinesterase enzyme. This action may be explained by the non-competitive behavior of compound 5476423 against acetylcholinesterase enzyme.
Alzheimer's disease, acetylcholinesterase, 8-hydroxyquinoline, in silico, non-competitive