Design and evaluation of selective butyrylcholinesterase inhibitors based on Cinchona alkaloid scaffold
Fig 3
Representative inhibition experiment of BChE inhibited by CN-Bzl and AChE inhibited by CD-(mCl).
Points indicate the average apparent enzyme-inhibitor constant (Ki,app) at a given substrate (acetylthiocholine; ATCh) concentration according to the Hunter-Downs equation. The lines derived from linear regression analysis and y-intercept represent the enzyme-inhibitor dissociation constant Ki. The concentrations of CN-Bzl and CD-(mCl) used in experiments were 2–10 μM and 10–40 μM, respectively. For BChE and CN-Bzl determined enzyme-inhibitor dissociation constant (Ki) and enzyme-substrate dissociation constant (Ks) were 2.9±0.3 μM and 0.29±0.04 mM, respectively. For AChE and CD-(mCl) determined Ki and Ks constants were 23±1 μM and 0.74±0.08 mM.