Molecular dynamics simulation of Axillaridine–A: A potent natural cholinesterase inhibitor

Figures & data

Figure 1.  Natural AChE inhibitor, Axillaridine-A.

Figure 2.  Axillaridine–A located at the aromatic gorge of AChE (PDB code: 1B41) after 2-ns MD simulation. Only the active site amino acids are labeled for the sake of clarity.

Figure 3.  Important amino acid residues within 5.0 å at the active site of AChE after 2-ns MD simulation. For detail refer to the text.

Figure 4.  Size (Å) of the aromatic gorge between Glu₈₁/Try₂₈₆ (Upper) and Phe₃₃₈/Trp₈₆ (Lower) during 2-ns AChE-Axillaridine-A simulation.

Figure 5.  Stable π–π interactions between Trp₂₈₆/Tyr₇₂ (Lower) and the aromatic ring of Axillaridine–A/Tyr₁₂₄ (Upper) as a function of time in the AChE-Axillaridine-A simulation.

Figure 6.  π-π Interaction between the aromatic ring of Axillaridine-A (shown in gray color) and that of the Tyr124 residue (shown in orange color).

Table 1.  Summary of the average distances between heavy atoms (Å) for important stable hydrogen-bonding interactions between active site residues.

Hydrogen Bond	Distance (Å)
	protein	complex
His436 : NδH – Glu323 : O_2	4.80	2.80
Ser196 : OγH – His436 : N_2	2.80	2.90
Asp68 : NH – Asn81 : Oδ1	4.20	3.20
Ser77 : NH – Phe74 : O	3.00	3.80
Phe71 : NH – Asp68 : Oδ2	2.50	4.30
Ser77 : OγH – Asp68 : Oδ2	2.65	3.50
Asn81 : NH – Ser77 : O	2.90	3.10
Gln70 : NH – Asp68 : Oδ1	3.24	3.20
Ser282 OγH – Asp281 : O	4.30	3.00
Trp80 : NH – Ser77 : O	3.00	3.10
Tyr330 : OH – Ser77 : Oγ	2.90	4.80
Tyr330 : NH – Phe327 : O	3.40	3.00
Tyr66 : NH – Tyr117 : O	3.25	3.05