Virtual Screening and Biological Evaluation of Piperazine Derivatives as Human Acetylcholinesterase Inhibitors

Table 4

The residues from each HuAChE active site subsites (Wiesner et al., [27]) and its interaction with derivatives at catalytic site docking.

Biologically active sites of HuAChE	Residues	Catalytic site docking
		K	S1	S3	S4	S7
Catalytic triad	Ser 203	—	—	—	—	—
	Glu 334	—	—	—	—	—
	His 447	—	H-bond	H-bond	—	—
Oxyanion hole	Gly 121	Hydrophobic	Hydrophobic	Hydrophobic	Hydrophobic	—
	Gly 122	—	—	—	—	—
	Ala 204	—	—	—	—	—
Anionic subsite	Trp 86	—	Hydrophobic	Hydrophobic	—	Hydrophobic
	Tyr 133	—	—	—	—	—
	Gly 202	—	—	—	—	Hydrophobic
	Gly 448	—	—	—	—	Hydrophobic
	Ile 451	—	—	—	—	—
Acyl binding pocket	Trp 236	—	—	—	—	—
	Phe 295	—	—	Hydrophobic	Hydrophobic	—
	Phe 297	Hydrophobic	Hydrophobic	Hydrophobic	Hydrophobic	Hydrophobic
	Phe 338	Hydrophobic	Hydrophobic	—	Hydrophobic	Hydrophobic
Peripheral anionic site	Asp 74	—	—	—	—	—
	Tyr 124	—	—	–-	Hydrophobic	—
	Ser 125	—	Hydrophobic	H-bond	Hydrophobic	—
	Trp 286	Hydrophobic	—	—	—	—
	Tyr 337	H-bond	H-bond	H-bond	Hydrophobic	Hydrophobic
	Tyr 341	Hydrophobic	Hydrophobic	—	Hydrophobic	Hydrophobic