Pancreatic lipase inhibition activity of trilactone terpenes of Ginkgo biloba

Figures & data

Figure 1.  Structural formulas of terpene trilactones (TTLs): ginkgolides and bilobalide.

Figure 2.  (A) Comparison between the docked pose (green) of the ligand CllP as produced by docking simulation and the crystallographic structure of this ligand (red) within the binding pocket of PL. (B) The solvent accessible surface area of the binding site of PL (1LPB) and the co-crystallized inhibitor (CllP).

Table 1.  The docked G. biloba terpene trilactones (TTLs) with their IC₅₀ values ranked according to the estimated binding affinity.

Rank^*	TTLs	Chemgauss2 score	IC50 (µg/mL)
1	Ginkgolide A	53.92	22.9
2	Ginkgolide L	53.76	—
3	Bilobalide	42.62	60.1
4	Ginkgolide J	41.20	-
5	Ginkgolide B	37.55	90.0
6	Ginkgolide K	34.24	—
7	Ginkgolide C	32.22	inactive

*Rank: Estimated binding affinity-rank calculated using Chemgauss2 scoring functions.

Figure 3.  (A) Detailed view of the co-crystallized structure (CllP) and the corresponding interacting amino acids within the binding site of pancreatic lipase (PL) (PDB code: 1LPB). (B) Detailed view of the docked ginkgolide A (G-A) structure and the corresponding interacting amino acid moieties within the binding site of PL. (C) Detailed view of the docked bilobalide–PL interactions. (D) Detailed view of the docked ginkgolide C–PL interactions.