当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > The inefficacy of donepezil on glycated-AChE inhibition: Binding affinity, complex stability and mechanism.

The inefficacy of donepezil on glycated-AChE inhibition: Binding affinity, complex stability and mechanism.

Abstract：

:Donepezil (DPZ) is a well-known drug for Alzheimer's disease that inhibits acetylcholinesterase activity (AChE). In the present study, the inhibitory effect of DPZ on non-enzymatic glycated-AChE (GLY-AChE) was studied by different experimental and simulation techniques. The initial investigation revealed that glycation process could reduce AChE activity approximately 60% in the pure enzyme and 38% in the extracted crude AChE from neural cells cultured in the presence of high glucose (HG) concentration. It is suggested that glycation of lysine residues on the structure of AChE could change the conformation of the active site (Trp-86 and His-447) in a way that the orientation of acetylcholine interrupted. The further studies indicated that DPZ is although a strong inhibitor for the native enzyme, it is not able to affect the GLY-AChE activity. The KD values of AChE-DPZ and GLY-AChE-DPZ complexes were estimated to be 1.88 × 10-9 and 2.10 × 10-6, respectively. The stability assessment showed that AChE-DPZ complex is more stable than the glycated complex. Our results indicate that, glycation process could impact on the conformation of the residues involved in the DPZ binding cavity on α-helix domain. Therefore, DPZ is not able to bind its specific cavity to induce its inhibitory effects on GLY-AChE.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Yekta R,Sadeghi L,Dehghan G

doi

10.1016/j.ijbiomac.2020.05.177

subject

Has Abstract

pub_date

2020-10-01 00:00:00

pages

35-46

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)33335-3

journal_volume

160

pub_type

杂志文章

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