Chemometric guided isolation of new triterpenoid saponins as acetylcholinesterase inhibitors from seeds of Achyranthes bidentata Blume.

Achyranthes bidentata Blume (Amaranthaceae) is an annual or perennial herb widely used as ethnomedicine in Traditional Chinese Medicine for treating fever, cold, ulcers, mensural pain, dementia, and osteoporosis. In the current study, UPLC-IM-Q-TOF-MS/MS-based chemometric approach was adopted for the tentative identification of fifty-six compounds in the extract and fractions of A.bidentata seeds. Further, the chemometric-guided isolation led to the isolation of two previously undescribed oleanane-type triterpenoid saponins, named achyranosides A-B (27 and 30), along with three known compounds (31 , 44 , and 23) from water fraction of A. bidentata seeds. The structures of new compounds were elucidated based on the detailed analysis of NMR, HR-ESI-MS, FT-IR spectral data, and GC-FID techniques. The isolated compounds in vitro acetylcholinesterase inhibitory activity revealed the promising activity of chikusetsusaponin IVa (23) (IC 50 = 63.7 μM) with mixed type of AChE inhibition in enzyme kinetic studies. Additionally, in silico binding free energy of isolated compounds disclosed the greater stability of enzyme-ligand complex owing to underlying multiple H-bond interactions. Overall, the study demonstrates the effectiveness of a chemometric-guided approach for the phytochemical exploration and isolation of new oleanane-type triterpenoid saponins from A. bidentata seeds. [Display omitted] • Fifty-six compounds were tentatively identified in the extract and fractions of A. bidentata seeds using UPLC-IM-Q-TOF-MS/MS analysis. • Two previously undescribed triterpenoid saponins along with three known were isolated from water fraction using chemometric-guided isolation. • The extract, fractions and isolated saponins demonstrated encouraging in vitro acetylcholinesterase inhibitory potential and greater stability of enzyme-inhibitor complex in in silico studies. • Chikusetsusaponin IVa [(5); IC 50 : 63.72 μM] showed mixed type of AchE inhibition in the enzyme kinetic studies. [ABSTRACT FROM AUTHOR]