Search results for "Clerodane Diterpenes"
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Complete 1H and 13C NMR assignments of clerodane diterpenoids of Salvia splendens.
2006
Unambiguous and complete assignments of 1H and 13C NMR chemical shifts for five clerodane diterpenes, four of them isolated from Salvia splendens (salviarin, splendidin and splenolides A and B) and one obtained by acetylation of splenolide A, are presented. The assignments are based on 2D shift-correlated [1H,1H–COSY, 1H,13C-gHSQC–1J(C,H) and 1H,13C-gHMBC-nJ(C,H) (n = 2 and 3)] and nuclear Overhauser effect (NOE) experiments. The conformation of the rings of these compounds is supported by the 3J(H,H) values and NOE results. Copyright © 2006 John Wiley & Sons, Ltd.
Cytotoxic neo-clerodane diterpenes from Stachys aegyptiaca
2018
Abstract Two new E/Z neo-clerodane diterpene isomers, trivially named stachaegyptin D (1) and E (2), together with known compounds, stachysolon monoacetate (3) and stachysolon diacetate (4), were isolated from an organic-solvent extract of the medicinal herb Stachys aegyptiaca. Structures were elucidated by a combination of spectroscopic methods, including HREIMS, 1H, 13C, DEPT, and 2D NMR analysis, as well as, first time X-ray analysis for stachysolone (3). All isolated metabolites showed some activity against the human hepatocellular cell line, HepG2. Compound 4 was the most active with an IC50 of 59.5 μM.
Synthetic studies on neoclerodane diterpenes from Salvia splendens: oxidative modifications of ring A.
2011
Salvinorin A (1), a neoclerodane diterpene from the hallucinogenic mint Salvia divinorum, is the only known naturally occurring non-nitrogenous and specific κ-opioid agonist. Some oxidative modifications of the A ring in the congeners of 1 isolated from Salvia splendens salviarin, splenolide B, splendidin and in the non-natural 8-epi-salviarin gave new derivatives, some of which were tested as agonists at opioid receptors. However, none of these compounds were active. The presence of the C-18, C-19 lactone could be at the origin of the observed lack of binding affinity.