Table 1.
Cholinesterases inhibitory activities, inhibition type, and dissociation constants (Ki) of zerumbone.
| Sample | AChE | BChE | ||||
|---|---|---|---|---|---|---|
| IC50 1 | Ki Value 2 | Inhibition Type 3 |
IC50 | Ki Value | Inhibition Type |
|
| Zerumbone | 2.78 ± 0.48 | 3.5 | Non-competitive | 4.12 ± 0.42 | 3.8 | Competitive |
| Galantamine 4 | 1.50 ± 0.05 | - | Competitive | 14.47 ± 0.33 | Competitive 5 | |
1 IC50 (µM) was indicated as a mean ± standard deviation (SD) of the independent triplicate experiments. 2 The inhibition constants (Ki, µM) represented the binding affinity between the inhibitor and the enzyme. 3 The inhibition type was obtained by Dixon and Lineweaver-Burk plots. 4 Galantamine was used as a positive control in the cholinesterase assays. 5 Ref. Synthesis and Evaluation of the Biological Profile of Novel Analogues of Nucleosides and of Potential Mimetics of Sugar Phosphates and Nucleotides. 2015. Xavier et al. (-) Not tested.