naringenin-chalcone and isoliquiritigenin

naringenin-chalcone has been researched along with isoliquiritigenin* in 2 studies

Other Studies

2 other study(ies) available for naringenin-chalcone and isoliquiritigenin

Article	Year
Cytotoxic Evaluation against Breast Cancer Cells of Isoliquiritigenin Analogues from Spatholobus suberectus and Their Synthetic Derivatives. Journal of natural products, 2016, Jan-22, Volume: 79, Issue:1 Five isoliquiritigenin analogues, including a new methylene-bridged bischalcone (1), were isolated from Spatholobus suberectus. Cytotoxicity screening of these isolates and several synthetic derivatives indicated that the introduction, removal, position modification, or glycosylation of hydroxy groups in isoliquiritigenin did not improve the resultant cytotoxicity against the MCF-7 and MDA-MB-231 human breast cancer cell lines. In addition, cyclization of OH-2' chalcones or reduction of the α,β-unsaturated carbonyl double bond decreased such cytotoxicity substantially. However, methylation of hydroxy groups resulted in a marked increase in such cytotoxic activity. Among these active isoliquiritigenin analogues, 3',4',5',4″-tetramethoxychalcone (3h) was obtained as a compound with promising cytotoxic activity. Topics: Antineoplastic Agents, Phytogenic; Breast Neoplasms; Cell Proliferation; Chalcones; Drug Screening Assays, Antitumor; Drugs, Chinese Herbal; Fabaceae; Female; Humans; Molecular Structure	2016
First bacterial chalcone isomerase isolated from Eubacterium ramulus. Archives of microbiology, 2004, Volume: 181, Issue:6 The human fecal anaerobe Eubacterium ramulus is capable of degrading various flavonoids, including the flavone naringenin. The first step in the proposed degradation pathway is the isomerization of naringenin to the corresponding chalcone. Cell-free extracts of E. ramulus displayed chalcone isomerase activity. The enzyme from E. ramulus was purified to homogeneity. Its apparent molecular mass was estimated to be 136 and 129 kDa according to gel filtration and native polyacrylamide gel electrophoresis, respectively. Chalcone isomerase is composed of one type of subunit of 30 kDa. The purified enzyme catalyzed the isomerization of naringenin chalcone, isoliquiritigenin, and butein, three chalcones that differ in their hydroxylation pattern. N-bromosuccinimide, but also naringenin and phloretin, inhibited the purified enzyme considerably. This is the first report on a bacterial chalcone isomerase. The physiological function of the purified enzyme is unclear, but an involvement in the conversion of the flavanone naringenin to the chalcone is proposed. Topics: Bromosuccinimide; Chalcone; Chalcones; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Eubacterium; Flavanones; Flavonoids; Intramolecular Lyases; Isomerism; Molecular Weight; Phloretin; Protein Subunits; Substrate Specificity	2004

Article

Year

Cytotoxic Evaluation against Breast Cancer Cells of Isoliquiritigenin Analogues from Spatholobus suberectus and Their Synthetic Derivatives.

Journal of natural products, 2016, Jan-22, Volume: 79, Issue:1

Five isoliquiritigenin analogues, including a new methylene-bridged bischalcone (1), were isolated from Spatholobus suberectus. Cytotoxicity screening of these isolates and several synthetic derivatives indicated that the introduction, removal, position modification, or glycosylation of hydroxy groups in isoliquiritigenin did not improve the resultant cytotoxicity against the MCF-7 and MDA-MB-231 human breast cancer cell lines. In addition, cyclization of OH-2' chalcones or reduction of the α,β-unsaturated carbonyl double bond decreased such cytotoxicity substantially. However, methylation of hydroxy groups resulted in a marked increase in such cytotoxic activity. Among these active isoliquiritigenin analogues, 3',4',5',4″-tetramethoxychalcone (3h) was obtained as a compound with promising cytotoxic activity.

Topics: Antineoplastic Agents, Phytogenic; Breast Neoplasms; Cell Proliferation; Chalcones; Drug Screening Assays, Antitumor; Drugs, Chinese Herbal; Fabaceae; Female; Humans; Molecular Structure

2016

First bacterial chalcone isomerase isolated from Eubacterium ramulus.

Archives of microbiology, 2004, Volume: 181, Issue:6

The human fecal anaerobe Eubacterium ramulus is capable of degrading various flavonoids, including the flavone naringenin. The first step in the proposed degradation pathway is the isomerization of naringenin to the corresponding chalcone. Cell-free extracts of E. ramulus displayed chalcone isomerase activity. The enzyme from E. ramulus was purified to homogeneity. Its apparent molecular mass was estimated to be 136 and 129 kDa according to gel filtration and native polyacrylamide gel electrophoresis, respectively. Chalcone isomerase is composed of one type of subunit of 30 kDa. The purified enzyme catalyzed the isomerization of naringenin chalcone, isoliquiritigenin, and butein, three chalcones that differ in their hydroxylation pattern. N-bromosuccinimide, but also naringenin and phloretin, inhibited the purified enzyme considerably. This is the first report on a bacterial chalcone isomerase. The physiological function of the purified enzyme is unclear, but an involvement in the conversion of the flavanone naringenin to the chalcone is proposed.

Topics: Bromosuccinimide; Chalcone; Chalcones; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Eubacterium; Flavanones; Flavonoids; Intramolecular Lyases; Isomerism; Molecular Weight; Phloretin; Protein Subunits; Substrate Specificity

2004