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1.
Appl Biochem Biotechnol ; 194(12): 5607-5626, 2022 Dec.
Article in English | MEDLINE | ID: mdl-35796948

ABSTRACT

The present study was designed to isolate a potential compound from the extracts of Elytraria acaulis (E. acaulis) for ovarian cancer. n-Hexane, ethyl acetate, chloroform, acetone and methanol extract were taken using the Soxhlet method. Thin layer, column chromatography, NMR and MASS studies were done for the isolation and structural characterization of the compound. Finally, the novel compound (Z)-3-(2-methyl-3-oxoprop-1-en-1-yl) phenyl heptanoate was identified. MTT assay, cell morphology and cell cycle analysis were done to evaluate the anticancer property of the compound. In the MTT assay, the percentage of the cell viability treated with the isolated compound was decreased while increasing the concentration of the compound. Cancer cells treated with the isolated compound showed distinct morphological changes when compared to the control untreated cells. In the cell cycle analysis, the isolated compound induced a significant increase in the percentage of cells in G0/G1 phase and a decrease in the percentage of cells in the S phase and G2-M phase of the PA 1 cell lines. The cell cycle arrest induced by the isolated compound may account for its antiproliferative capacity. Hence, the novel compound isolated from E. acaulis can be a potent candidate in the designing of anticancer drugs.


Subject(s)
Apoptosis , Ovarian Neoplasms , Humans , Female , Cell Proliferation , Ovarian Neoplasms/drug therapy , Ovarian Neoplasms/metabolism , Plant Leaves/metabolism , Cell Survival , Plant Extracts/chemistry
2.
Sci Rep ; 11(1): 11451, 2021 06 01.
Article in English | MEDLINE | ID: mdl-34075089

ABSTRACT

Matrix metalloproteinases (MMPs) are pivotal for cancer cell migration and metastasis which are generally over-expressed in such cell types. Many drugs targeting MMPs do so by binding to the conserved catalytic domains and thus exhibit poor selectivity due to domain-similarities with other proteases. We report herein the binding of a novel compound [3-(E-3,4-dihydroxycinnamaoyloxyl)-2-hydroxypropyl 9Z, 12Z-octadeca-9, 12-dienoate; Mol. wt: 516.67 Da], (C1), isolated from a seagrass, Cymodocea serrulata to the unconserved hemopexin-like (PEX) domain of MMP2 (- 9.258 kcal/mol). MD simulations for 25 ns, suggest stable ligand-target binding. In addition, C1 killed an ovarian cancer cell line, PA1 at IC50: 5.8 µM (lesser than Doxorubicin: 8.6 µM) and formed micronuclei, apoptotic bodies and nucleoplasmic bridges whilst causing DNA laddering, S and G2/M phase dual arrests and MMP disturbance, suggesting intrinsic apoptosis. The molecule increased mRNA transcripts of BAX and BAD and down-regulated cell survival genes, Bcl-xL, Bcl-2, MMP2 and MMP9. The chemical and structural details of C1 were deduced through FT-IR, GC-MS, ESI-MS, 1H and 13C NMR [both 1D and 2D] spectra.


Subject(s)
Alismatales/chemistry , Cinnamates , Esters , Linoleic Acid , Matrix Metalloproteinase 2/metabolism , Matrix Metalloproteinase Inhibitors , Animals , CHO Cells , Cell Cycle/drug effects , Cinnamates/chemistry , Cinnamates/isolation & purification , Cinnamates/pharmacology , Cricetulus , Esters/chemistry , Esters/isolation & purification , Esters/pharmacology , Linoleic Acid/chemistry , Linoleic Acid/isolation & purification , Linoleic Acid/pharmacology , Matrix Metalloproteinase Inhibitors/chemistry , Matrix Metalloproteinase Inhibitors/isolation & purification , Matrix Metalloproteinase Inhibitors/pharmacology , Protein Domains
3.
Sci Rep ; 9(1): 5992, 2019 04 12.
Article in English | MEDLINE | ID: mdl-30979908

ABSTRACT

In this paper, we describe the isolation of an unusual type of high molecular weight monorhamnolipid attached to esters of palmitic, stearic, hexa and octadecanoic acids as against the routinely reported di-rhamnolipids linked to hydroxydecanoic acids. The bioemulsifier was column-purified and the chemical nature of the compound was elucidated using FT-IR, GC-MS and 1D [1H and13C] and 2D NMR. This monorhamnolipid is extracted from a bacterium, Pseudomonas guganensis and is not reported to have biological activities, let alone emulsification abilities. The bacterium continually produced rhamnolipids when nourished with n-hexadecane as its lone carbon source. The extracellularly secreted monorhamnolipids are capable of degrading hydrocarbons, with most preference to n-hexadecane [EI24 of 56 ± 1.42% by 2 mL of the spent medium]. Whilst the crude ethyl acetate partitioned extract had an EI24 of 65 ± 1.43%; the purified rhamnolipid product showed 78 ± 1.75% both at 12.5 mg/mL concentration. The used-up n-hexadecane is biotransformed to prepare its own rhamnolipids which in return is utilized to degrade n-alkanes thus creating a circular pathway which is proposed herein. This bacterium can be seen as a new source of bioemulsifier to reduce hydrocarbon in polluted waters.


Subject(s)
Glycolipids/biosynthesis , Glycolipids/chemistry , Pseudomonas/metabolism , Emulsions , India , Pseudomonas/isolation & purification
4.
Phytomedicine ; 51: 196-204, 2018 Dec 01.
Article in English | MEDLINE | ID: mdl-30466617

ABSTRACT

BACKGROUND: Cardiovascular disease and its related deaths are increasing in the modern world. Therefore, there is a need to identify a plant based nutraceutical supplement with potent activity. HYPOTHESIS/PURPOSE: Reportedly, the protective effect of the rutin in hypoxia-induced cardiomyocytes is due to the activation of molecular networks related to programmed cell death. STUDY DESIGN-METHODS: Phytochemical methods and advanced analytical methods were employed to isolate natural products from Spermococe hispida their effects in cardiomyocyets. RESULTS: We reports herein that CoCl2-induced hypoxic condition significantly decreased cell viability as evidenced by MTT assay and cell cycle analysis. Western blot studies revealed an up-regulation of HIF-1α, BAX and caspase and down-regulation of BCl-2 expression, followed by modulation of Akt, p-Akt, p38 and p-p38. The oxidative abnormalities were ameliorated by rutin pretreatment, as deduced by the reduced CoCl2-induced cytotoxicity, MDA concentration and LDH activity and the enhanced levels of GSH and SOD in a dose-dependent manner. Rutin protects H9c2 cells from CoCl2-induced hypoxic damage by mitigating oxidative stress and preserving cell viability by modulating the antiapoptotic proteins. CONCLUSION: The overall findings reinforce the cardioprotective action of rutin, a potential source of antioxidant of natural origin, which may help in mitigating the progress of oxidative stress in hypoxic conditions such as myocardial infarction and stroke.


Subject(s)
Apoptosis/drug effects , Myocytes, Cardiac/drug effects , Oxidative Stress/drug effects , Protective Agents/pharmacology , Rutin/pharmacology , Animals , Antioxidants/pharmacology , Cell Hypoxia/drug effects , Cell Line , Cell Survival/drug effects , Cobalt , Plant Components, Aerial/chemistry , Rats , Rubiaceae/chemistry
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