Browse
Submit Data
Databases
API
Help

Dataset Information

5 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Synergistic Contribution of Tiglate and Cinnamate to Cytotoxicity of Ipomoeassin F.

ABSTRACT: An efficient synthetic route for ipomoeassin F and its tiglate-modified analogues was developed. The route features late-stage conformation-controlled highly regioselective esterification of the glucose diol in the disaccharide core. The results from the NCI-60 cell line screens of ipomoeassin F were reported for the first time. Moreover, two new C-3-cinnamoyl-Glcp analogues (2 and 3) were prepared. Their in-house cytotoxicity data convey an important message that both identity and positioning of the two ?,?-unsaturated esters are crucial. They are not interchangeable.

SUBMITTER: Zong G

PROVIDER: S-EPMC5483335 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Synergistic Contribution of Tiglate and Cinnamate to Cytotoxicity of Ipomoeassin F.

Zong Guanghui G Whisenhunt Lucas L Hu Zhijian Z Shi Wei Q WQ

The Journal of organic chemistry 20170417 9

An efficient synthetic route for ipomoeassin F and its tiglate-modified analogues was developed. The route features late-stage conformation-controlled highly regioselective esterification of the glucose diol in the disaccharide core. The results from the NCI-60 cell line screens of ipomoeassin F were reported for the first time. Moreover, two new C-3-cinnamoyl-Glcp analogues (2 and 3) were prepared. Their in-house cytotoxicity data convey an important message that both identity and positioning o ...[more]

PMID: 28394135

Similar Datasets

Cinnamate-based DNA photolithography.

Project description:As demonstrated by means of DNA nanoconstructs, as well as DNA functionalization of nanoparticles and micrometre-scale colloids, complex self-assembly processes require components to associate with particular partners in a programmable fashion. In many cases the reversibility of the interactions between complementary DNA sequences is an advantage. However, permanently bonding some or all of the complementary pairs may allow for flexibility in design and construction. Here, we show that the substitution of a cinnamate group for a pair of complementary bases provides an efficient, addressable, ultraviolet light-based method to bond complementary DNA covalently. To show the potential of this approach, we wrote micrometre-scale patterns on a surface using ultraviolet light and demonstrated the reversible attachment of conjugated DNA and DNA-coated colloids. Our strategy enables both functional DNA photolithography and multistep, specific binding in self-assembly processes.

| S-EPMC3722280 | biostudies-literature

Contribution of 6mer seed toxicity to HIV-1 induced cytotoxicity

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-06-07 | GSE218195 | GEO

Creatininium cinnamate.

Project description:THE CRYSTAL STRUCTURE OF THE TITLE COMPOUND (SYSTEMATIC NAME: 2-amino-1-methyl-4-oxo-4,5-dihydro-1H-imidazol-3-ium 3-phenyl-prop-2-enoate), C(4)H(8)N(3)O(+)·C(9)H(7)O(2) (-), is stabilized by N-H?O hydrogen bonding. Cations are linked to anions to form ion pairs with an R(2) (2)(8) ring motif. These ion pairs are connected through a C(2) (2)(6) chain motif extending along the c axis of the unit cell. This crystal packing is characterized by hydro-phobic layers at x ? 1/2 packed between hydro-philic layers at x ? 0.

| S-EPMC3120415 | biostudies-other

Synergistic cytotoxicity of gemcitabine, clofarabine and edelfosine in lymphoma cell lines.

Project description:Treatments for lymphomas include gemcitabine (Gem) and clofarabine (Clo) which inhibit DNA synthesis. To improve their cytotoxicity, we studied their synergism with the alkyl phospholipid edelfosine (Ed). Exposure of the J45.01 and SUP-T1 (T-cell) and the OCI-LY10 (B-cell) lymphoma cell lines to IC10-IC20 levels of the drugs resulted in strong synergistic cytotoxicity for the 3-drug combination based on various assays of cell proliferation and apoptosis. Cell death correlated with increased phosphorylation of histone 2AX and KAP1, decreased mitochondrial transmembrane potential, increased production of reactive oxygen species and release of pro-apoptotic factors. Caspase 8-negative I9.2 cells were considerably more resistant to [Gem+Clo+Ed] than caspase 8-positive cells. In all three cell lines [Gem+Clo+Ed] decreased the level of phosphorylation of the pro-survival protein AKT and activated the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) stress signaling pathway, which in J45.01 cells resulted in the phosphorylation and heterodimerization of the transcription factors ATF2 and c-Jun. The observed rational mechanism-based efficacy of [Gem+Clo+Ed] based on the synergistic convergence of several pro-death and anti-apoptotic signaling pathways in three very different cell backgrounds provides a powerful foundation for undertaking clinical trials of this drug combination for the treatment of lymphomas.

| S-EPMC3913938 | biostudies-other

Ipomoeassin F Binds Sec61α to Inhibit Protein Translocation.

Project description:Ipomoeassin F is a potent natural cytotoxin that inhibits growth of many tumor cell lines with single-digit nanomolar potency. However, its biological and pharmacological properties have remained largely unexplored. Building upon our earlier achievements in total synthesis and medicinal chemistry, we used chemical proteomics to identify Sec61α (protein transport protein Sec61 subunit alpha isoform 1), the pore-forming subunit of the Sec61 protein translocon, as a direct binding partner of ipomoeassin F in living cells. The interaction is specific and strong enough to survive lysis conditions, enabling a biotin analogue of ipomoeassin F to pull down Sec61α from live cells, yet it is also reversible, as judged by several experiments including fluorescent streptavidin staining, delayed competition in affinity pulldown, and inhibition of TNF biogenesis after washout. Sec61α forms the central subunit of the ER protein translocation complex, and the binding of ipomoeassin F results in a substantial, yet selective, inhibition of protein translocation in vitro and a broad ranging inhibition of protein secretion in live cells. Lastly, the unique resistance profile demonstrated by specific amino acid single-point mutations in Sec61α provides compelling evidence that Sec61α is the primary molecular target of ipomoeassin F and strongly suggests that the binding of this natural product to Sec61α is distinctive. Therefore, ipomoeassin F represents the first plant-derived, carbohydrate-based member of a novel structural class that offers new opportunities to explore Sec61α function and to further investigate its potential as a therapeutic target for drug discovery.

| S-EPMC6627486 | biostudies-literature

Synergistic cytotoxicity of perifosine and ABT-737 to colon cancer cells.

Project description:An acidic environment and hypoxia within the tumour are hallmarks of cancer that contribute to cell resistance to therapy. Deregulation of the PI3K/Akt pathway is common in colon cancer. Numerous Akt-targeted therapies are being developed, the activity of Akt-inhibitors is, however, strongly pH-dependent. Combination therapy thus represents an opportunity to increase their efficacy. In this study, the cytotoxicity of the Akt inhibitor perifosine and the Bcl-2/Bcl-xL inhibitor ABT-737 was tested in colon cancer HT-29 and HCT-116 cells cultured in monolayer or in the form of spheroids. The efficacy of single drugs and their combination was analysed in different tumour-specific environments including acidosis and hypoxia using a series of viability assays. Changes in protein content and distribution were determined by immunoblotting and a "peeling analysis" of immunohistochemical signals. While the cytotoxicity of single agents was influenced by the tumour-specific microenvironment, perifosine and ABT-737 in combination synergistically induced apoptosis in cells cultured in both 2D and 3D independently on pH and oxygen level. Thus, the combined therapy of perifosine and ABT-737 could be considered as a potential treatment strategy for colon cancer.

| S-EPMC9806293 | biostudies-literature

Contribution of 6mer seed toxicity to HIV-1 induced cytotoxicity (DISE-69)

Project description:Analysis of total RNA by RNA seq

2023-06-07 | GSE218194 | GEO

Contribution of 6mer seed toxicity to HIV-1 induced cytotoxicity [DISE-56]

Project description:Analysis of RISC bound short (s)RNAs in cells infected with HIV-1 reveals a contribution of 6mer seed toxicity to HIV-1 induced cytopathicity

2023-06-07 | GSE218193 | GEO

Contribution of 6mer seed toxicity to HIV-1 induced cytotoxicity (DISE-45)

Project description:Analysis of RISC bound short (s)RNAs in cells infected with HIV-1 reveals a contribution of 6mer seed toxicity to HIV-1 induced cytopathicity

2023-06-07 | GSE218192 | GEO

Contribution of 6mer seed toxicity to HIV-1 induced cytotoxicity [DISE-42]

Project description:Analysis of RISC bound short (s)RNAs in cells infected with HIV-1 reveals a contribution of 6mer seed toxicity to HIV-1 induced cytopathicity

2023-06-07 | GSE218191 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data