Chemical Constituents of Equisetum Debile and their Cytotoxic Activity

A new phenyl glycoside, equisetumoside D (1), was isolated from the aerial parts of Equisetum debile, along with equisetumoside B (2), dehydrovomifoliol (3), corchoionoside C (4), (-)-isolariciresinol-3a-O-β-D-glucopyranoside (5), and kaempferol 3-O-sophoroside-7-O-β-D-glucopyranoside (6). Their structures were elucidated by NMR spectroscopic and MS experiments. Compound 1 was found to be cytotoxic against both tested human cancer cell lines, hepatocellular carcinoma (Hep-G2, IC50: 1.12 μg/mL) and rhabdosarcoma (RD, IC50: 0.25 μg/mL), while the other compounds showed no activity against these cell lines by in vitro assay.

Download Full-text

In vitro anticancer potential of aerial parts of Ipomoea horsfalliae hook in different human cancer cell lines

Industrial Crops and Products ◽

10.1016/j.indcrop.2020.112746 ◽

2020 ◽

Vol 155 ◽

pp. 112746

Author(s):

VK Muhammed Ashraf ◽

V.K. Kalaichelvan ◽

V.V. Venkatachalam ◽

R. Ragunathan

Keyword(s):

Cell Lines ◽

Cancer Cell ◽

Human Cancer ◽

Cancer Cell Lines ◽

Human Cancer Cell ◽

Human Cancer Cell Lines ◽

Aerial Parts

Download Full-text

Developing and Evaluating In Vitro Effect of Poly(Ethylene Glycol) Conjugated Curcumin on Human Cancer Cell Lines

Current Drug Discovery Technologies ◽

10.2174/1570163813666161018131228 ◽

2016 ◽

Vol 13 (4) ◽

pp. 254-266 ◽

Cited By ~ 1

Author(s):

Bui Thanh Tung ◽

Nguyen Thanh Hai ◽

Phan Ke Son

Keyword(s):

Ethylene Glycol ◽

Cell Lines ◽

Cancer Cell ◽

Human Cancer ◽

Human Cancer Cell ◽

Poly Ethylene Glycol ◽

Human Cancer Cell Lines ◽

Poly Ethylene ◽

Vitro Effect

Download Full-text

Discovery of New Pyrazolopyridine, Furopyridine, and Pyridine Derivatives as CDK2 Inhibitors: Design, Synthesis, Docking Studies, and Anti-Proliferative Activity

Molecules ◽

10.3390/molecules26133923 ◽

2021 ◽

Vol 26 (13) ◽

pp. 3923

Author(s):

Adel A.-H. Abdel-Rahman ◽

Amira K. F. Shaban ◽

Ibrahim F. Nassar ◽

Dina S. EL-Kady ◽

Nasser S. M. Ismail ◽

...

Keyword(s):

Cell Lines ◽

Cancer Cell ◽

Human Cancer ◽

Cancer Cell Lines ◽

Human Cancer Cell ◽

Molecular Docking Study ◽

Human Cancer Cell Lines ◽

Hct 116 ◽

Mcf 7

New pyridine, pyrazoloyridine, and furopyridine derivatives substituted with naphthyl and thienyl moieties were designed and synthesized starting from 6-(naphthalen-2-yl)-2-oxo-4-(thiophen-2-yl)-1,2-dihydropyridine-3-carbonitrile (1). The chloro, methoxy, cholroacetoxy, imidazolyl, azide, and arylamino derivatives were prepared to obtain the pyridine-−C2 functionalized derivatives. The derived pyrazolpyridine-N-glycosides were synthesized via heterocyclization of the C2-thioxopyridine derivative followed by glycosylation using glucose and galactose. The furopyridine derivative 14 and the tricyclic pyrido[3′,2′:4,5]furo[3,2-d]pyrimidine 15 were prepared via heterocyclization of the ester derivative followed by a reaction with formamide. The newly synthesized compounds were evaluated for their ability to in vitro inhibit the CDK2 enzyme. In addition, the cytotoxicity of the compounds was tested against four different human cancer cell lines (HCT-116, MCF-7, HepG2, and A549). The CDK2/cyclin A2 enzyme inhibitory results revealed that pyridone 1, 2-chloro-6-(naphthalen-2-yl)-4-(thiophen-2-yl)nicotinonitrile (4), 6-(naphthalen-2-yl)-4-(thiophen-2-yl)-1H-pyrazolo[3,4-b]pyridin-3-amine (8), S-(3-cyano-6-(naphthaen-2-yl)-4-(thiophen-2-yl)pyridin-2-yl) 2-chloroethanethioate (11), and ethyl 3-amino-6-(naphthalen-2-yl)-4-(thiophen-2-yl)furo[2,3-b]pyridine-2-carboxylate (14) are among the most active inhibitors with IC50 values of 0.57, 0.24, 0.65, 0.50, and 0.93 µM, respectively, compared to roscovitine (IC50 0.394 μM). Most compounds showed significant inhibition on different human cancer cell lines (HCT-116, MCF-7, HepG2, and A549) with IC50 ranges of 31.3–49.0, 19.3–55.5, 22.7–44.8, and 36.8–70.7 μM, respectively compared to doxorubicin (IC50 40.0, 64.8, 24.7 and 58.1 µM, respectively). Furthermore, a molecular docking study suggests that most of the target compounds have a similar binding mode as a reference compound in the active site of the CDK2 enzyme. The structural requirements controlling the CDK2 inhibitory activity were determined through the generation of a statistically significant 2D-QSAR model.

Download Full-text