A first principle study on the interaction between acetylcholinesterase and acetylcholine, and also rivastigmine in alzheimer's disease case

6th Asian Physics Symposium

Khoirunisa, V.^1 ; Rusydi, F.^2 ; Kasai, H.^3 ; Gandaryus, A.G.^1 ; Dipojono, H.K.^1

Department of Engineering Physics, Institut Teknologi Bandung, Jl. Ganesha No. 10, Bandung

40132, Indonesia^1

Theoretical Physics Research Group, Department of Physics, Faculty of Science and Technology, Airlangga University, Kampus C, Jl. Mulyorejo, Surabaya

60115, Indonesia^2

Department of Precision Science and Technology and Applied Physics, Graduate School of Engineering, Osaka University, Osaka, Suita

565-0871, Japan^3

关键词: Acetylcholinesterase;    Acetylcholinesterase enzymes;    Alzheimer's disease;    Calculation results;    First-principle study;    First-principles calculation;    Rivastigmine;    Substrate interaction;   

Others  :  https://iopscience.iop.org/article/10.1088/1742-6596/739/1/012136/pdf
DOI  :  10.1088/1742-6596/739/1/012136

来源: IOP

【 摘 要 】

The catalytic activity of acetylcholinesterase enzyme (AChE) relates to the symptom progress in Alzheimer's disease. Interaction of AChE with rivastigmine (from the medicine) can reduce its catalytic activity toward acetylcholine to decelerate the progression of Alzheimer's disease. This research attempts to study the interaction between AChE and rivastigmine, and also acetylcholine (without the presence of rivastigmine) using density functional theory by simplifying the reaction occurs in the active site, which is assumed to be C2H5OH, C3N2H3(Ch3), and CH3COO-. The results suggest that AChE interacts easier with acetylcholine than with rivastigmine, which implies that the medicine does not effectively reduce the catalytic activity of AChE. At this stage, no experimental data is available to be compared with the calculation results. Nonetheless, this study has shown a good prospect to understand the AChE-substrate interaction using a first-principles calculation.