Metabolomic profile, anti-trypanosomal potential and molecular docking studies of Thunbergia grandifolia

Figures & data

Table 1. LC-HRESIMS-dereplicated phytochemicals in the methanol extract of Thunbergia grandifolia.

No.	Rt (min)	m/z	Ionisation mode	Calculated mass	Accurate mass	Molecular formula	Putative identification	Chemical class
1.	0.63	379.08225	Negative	380.08953	380.089605	C21H16O7	Diphyllin	Lignans
2.	3.40	254.22458	Positive	253.22458	254.224580	C16H30O2	6-Hexadecenoic acid	Fatty acid
3.	4.44	331.08196	Positive	330.07468	330.073955	C17H14O7	3,5,7-Trihydroxy-3′,4′-dimethoxyflavone	Flavonoids
4.	4.45	719.15891	Positive	718.15163	718.153390	C36H30O16	Rosmarinic acid dimer	Phenolic acids
5.	4.51	337.12848	Positive	336.1212	336.120905	C17H20O7	Avicennone B	Napthoquinones
6.	4.57	349.09262	Positive	348.10565	348.105649	C14H20O10	Stilbericoside	Iridoid glucosides
7.	5.34	333.10983	Negative	334.11711	334.126385	C14H22O9	Alatoside	Iridoid glucosides
8.	6.03	319.11782	Negative	320.1251	320.125990	C17H20O6	4-Deoxyavicennone B	Napthoquinones
9.	6.77	369.09494	Positive	368.08766	368.087412	C14H21ClO9	5-Deoxythunbergioside	Iridoid glucosides
10.	6.80	229.08642	Positive	228.07914	228.078645	C14H12O3	Naphtho[2,3-b]furan-4,9-diol; di-Me ether	Napthoquinones
11.	7.78	491.26569	Negative	492.27297	492.273656	C28H36N4O4	(+)-Aphelandrine	Alkaloids
12.	8.15	349.19842	Positive	348.14204	348.142035	C15H24O9	Thunaloside	Iridoid glucosides
13.	9.48	263.12852	Positive	262.12124	262.120509	C15H18O4	3a-Deoxyavicennone G	Napthoquinones
14.	9.51	285.07621	Positive	284.06894	284.068475	C16H12O5	5,7-Dihydroxy-4′-methoxyflavone	Flavonoids
15.	10.43	331.1905	Negative	332.11764	332.110735	C14H20O9	Isounedoside	Iridoid glucosides

Note: Rt: retention time; m/z: mass-to-charge ratio.

Figure 1. Chemical structures of identified compounds in the methanol extract of T. grandifolia.

Figure 2. Binding modes of diphyllin (left side) inside the active site of rhodesain target. Binding mode of co-crystalized ligand (right side) inside the active site of rhodesain.

Figure 3. Binding modes of avicennone B (left side) inside the active site of farnesyl diphosphate synthase target. Binding mode of co-crystalized ligand (right side) inside the active site of farnesyl diphosphate synthase.

Figure 4. RMSDs of diphyllin and avacennone B inside the active sites of rhodesain and farnesyl diphosphate synthase, respectively, over 50 ns of MDS.

Figure 5. Protein-ligand contacts inside the rhodesain’ and farnesyl diphosphate synthase’s binding sites over 50 ns of MDS: (A–D) diphyllin and avacennone B alongside the corresponding co-crystalized ligands, respectively.

Figure 6. In-silico predicted pharmacokinetic properties of diphyllin (A) and avacennone B (B).