• Media type: E-Article
  • Title: Structure Elucidation and Cholinesterase Inhibition Activity of Two New Minor Amaryllidaceae Alkaloids
  • Contributor: Maříková, Jana; Mamun, Abdullah Al; Shammari, Latifah Al; Korábečný, Jan; Kučera, Tomáš; Hulcová, Daniela; Kuneš, Jiří; Malaník, Milan; Vašková, Michaela; Kohelová, Eliška; Nováková, Lucie; Cahlíková, Lucie; Pour, Milan
  • Published: MDPI AG, 2021
  • Published in: Molecules
  • Extent: 1279
  • Language: English
  • DOI: 10.3390/molecules26051279
  • ISSN: 1420-3049
  • Keywords: Chemistry (miscellaneous) ; Analytical Chemistry ; Organic Chemistry ; Physical and Theoretical Chemistry ; Molecular Medicine ; Drug Discovery ; Pharmaceutical Science
  • Abstract: <jats:p>Two new minor Amaryllidaceae alkaloids were isolated from Hippeastrum × hybridum cv. Ferrari and Narcissus pseudonarcissus cv. Carlton. The chemical structures were identified by various spectroscopic (one- and two-dimensional (1D and 2D) NMR, circular dichroism (CD), high-resolution mass spectrometry (HRMS) and by comparison with literature data of similar compounds. Both isolated alkaloids were screened for their human acetylcholinesterase (hAChE) and butyrylcholinesterase (hBuChE) inhibition activity. One of the new compounds, a heterodimer alkaloid of narcikachnine-type, named narciabduliine (2), showed balanced inhibition potency for both studied enzymes, with IC50 values of 3.29 ± 0.73 µM for hAChE and 3.44 ± 0.02 µM for hBuChE. The accommodation of 2 into the active sites of respective enzymes was predicted using molecular modeling simulation.</jats:p>
  • Description: <jats:p>Two new minor Amaryllidaceae alkaloids were isolated from Hippeastrum × hybridum cv. Ferrari and Narcissus pseudonarcissus cv. Carlton. The chemical structures were identified by various spectroscopic (one- and two-dimensional (1D and 2D) NMR, circular dichroism (CD), high-resolution mass spectrometry (HRMS) and by comparison with literature data of similar compounds. Both isolated alkaloids were screened for their human acetylcholinesterase (hAChE) and butyrylcholinesterase (hBuChE) inhibition activity. One of the new compounds, a heterodimer alkaloid of narcikachnine-type, named narciabduliine (2), showed balanced inhibition potency for both studied enzymes, with IC50 values of 3.29 ± 0.73 µM for hAChE and 3.44 ± 0.02 µM for hBuChE. The accommodation of 2 into the active sites of respective enzymes was predicted using molecular modeling simulation.</jats:p>
  • Footnote:
  • Access State: Open Access