Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

3?,5?-Cyclocholestan-6?-yl ethers as donors of the cholesterol moiety for the electrochemical synthesis of cholesterol glycoconjugates.

ABSTRACT: 3?,5?-Cyclocholestan-6?-yl alkyl and aryl ethers were proved to be efficient cholesteryl donors in the electrochemical synthesis of glycoconjugates. 3?,5?-Cyclocholestan-6?-ol (i-cholesterol) and its tert-butyldimethylsilyl ether can also be used for this purpose. The i-cholesterol derivatives show similar reactivities to those of previously studied 3?,5?-cyclocholestan-6?-thioethers.

SUBMITTER: Tomkiel AM

PROVIDER: S-EPMC4362039 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

3α,5α-Cyclocholestan-6β-yl ethers as donors of the cholesterol moiety for the electrochemical synthesis of cholesterol glycoconjugates.

Tomkiel Aneta M AM Biedrzycki Adam A Płoszyńska Jolanta J Naróg Dorota D Sobkowiak Andrzej A Morzycki Jacek W JW

Beilstein journal of organic chemistry 20150126

3α,5α-Cyclocholestan-6β-yl alkyl and aryl ethers were proved to be efficient cholesteryl donors in the electrochemical synthesis of glycoconjugates. 3α,5α-Cyclocholestan-6β-ol (i-cholesterol) and its tert-butyldimethylsilyl ether can also be used for this purpose. The i-cholesterol derivatives show similar reactivities to those of previously studied 3α,5α-cyclocholestan-6β-thioethers. ...[more]

PMID: 25815065

Similar Datasets

(20S)-22-Iodo-methyl-6β-meth-oxy-3α,5-dihydro-3'H-cyclo-propa[3α,5]-5α-pregnane.

Project description:In the title steroid derivative, C(23)H(37)IO, the fused cyclo-propane unit that comprises part of the A ring has a β-configuration, and the associated cyclo-pentane ring has an envelope conformation.

| S-EPMC2981155 | biostudies-literature

6β-Acetamido-5α-hydroxy-cholestan-3β-yl acetate.

Project description:The title steroid, C(31)H(53)NO(4), was prepared from the corresponding 5α,6α-epoxy-cholestane. The conformation of the six-membered rings is close to a chair form, while the five-membered ring adopts a twist conformation. The hydroxyl and acetamide groups are in axial positions. The nucleophilic species bound to the steroid nucleus at position 6 by the β-face, whereas the hydroxyl group at position 5 has α-orientation. All rings are trans-fused. The crystal packing shows that the mol-ecules related by twofold symmetry exist as O-H⋯O hydrogen-bonded dimers.

| S-EPMC2959794 | biostudies-literature

3α,4α-Ep-oxy-5α-androstan-17β-yl acetate.

Project description:The title compound, C(21)H(32)O(3), results from modifications of the A and D rings of the aromatase substrate androstenedione. Ring A adopts a conformation between 10β-sofa and 1α,10β half-chair. Rings B and C are in slightly flattened chair conformations. Ring D approaches a 13β-envelope conformation, probably due to the acet-oxy substituent, and shows a very short Csp(3)-Csp(3) bond next to the epoxide ring, which is characteristic of 3-4 epoxides. .

| S-EPMC2968911 | biostudies-literature

6β-Chloro-5α-hydr-oxy-20-oxopregnan-3β-yl acetate.

Project description:The title steroid, C(23)H(35)ClO(4), is a pregnane derivative prepared by ring opening of the corresponding 5α,6α-ep-oxy steroid with BiCl(3). There are two symmetry-independent mol-ecules in the asymmetric unit that show no significant differences concerning bond lengths and angles. The conformation of the six-membered rings in both mol-ecules is close to a chair form, while the five-membered ring adopts an envelope conformation. All rings in both mol-ecules are trans-fused. The mol-ecules are held together by an extensive O-H⋯O hydrogen-bonding network.

| S-EPMC2962054 | biostudies-literature

Androstane-3β,5α,6β,17β-tetrol tri-hydrate.

Project description:The title hydrated tetrol, C(19)H(32)O(4)·3H(2)O, was synthesized by stereoselective reduction of the compound 3β,5α,6β-trihy-droxy-androstan-17-one. All rings are fused trans. The organic mol-ecules are connected head-to-tail along the c axis via O-H⋯O hydrogen bonds. Layers of water mol-ecules in the ab plane inter-connect these chains. A quantum chemical ab initio Roothan Hartree-Fock calculation of the isolated mol-ecule gives values for the mol-ecular geometry close to experimentally determined ones, apart from the C-O bond lengths, whose calculated values are significantly smaller than the measured ones, probably a consequence of the involvement of the C-OH groups in the hydrogen-bonding network.

| S-EPMC3151997 | biostudies-literature

(3α,5α)3-Hydroxypregnan-20-one (3α,5α-THP) Regulation of the HPA Axis in the Context of Different Stressors and Sex.

Project description:Corticotropin-releasing factor (CRF) regulates the stress response in the hypothalamus and modulates neurotransmission across the brain through CRF receptors. Acute stress increases hypothalamic CRF and the GABAergic neurosteroid (3α,5α)3-hydroxypregnan-20-one (3α,5α-THP). We previously showed that 3α,5α-THP regulation of CRF is sex and brain region dependent. In this study, we investigated 3α,5α-THP regulation of stress-induced hypothalamic CRF, CRF receptor type 1 (CRFR1), CRF binding protein (CRFBP), pro-opiomelanocortin (POMC), and glucocorticoid receptor (GR) by western blot and circulating corticosterone (CORT) by enzyme-linked immunosorbent assay (ELISA) in male and female Sprague Dawley rats. Tissue was collected after rats were injected with 3α,5α-THP (15 mg/kg, IP) or vehicle 15 min prior to 30 min of restraint stress (RS), or 10 min of forced swim stress (FSS) and 20 min recovery. The initial exposure to a stress stimulus increased circulating CORT levels in both males and females, but 3α,5α-THP attenuated the CORT response only in females after RS. 3α,5α-THP reduced GR levels in male and females, but differently between stressors. 3α,5α-THP decreased the CRF stress response after FSS in males and females, but after RS, only in female rats. 3α,5α-THP reduced the CRFR1, CRFBP, and POMC increases after RS and FSS in males, but in females only after FSS. Our results showed different stress responses following different types of stressors: 3α,5α-THP regulated the HPA axis at different levels, depending on sex.

| S-EPMC9406198 | biostudies-literature

(22E,24R)-3α,5-Cyclo-5α-ergosta-22-en-6-one.

Project description:In the title mol-ecule, C(28)H(44)O, the two six-membered rings have a chair conformation and the two five-membered rings haveenvelope conformations. The crystal packing exhibits no short inter-molecular contacts. The absolute configuration was assigned to correspond with that of the known chiral centres in a precursor molecule, which remained unchanged during the synthesis of the title compound.

| S-EPMC3051649 | biostudies-literature

Effect of a synthetic steroid 5α-androst-3β, 5α, 6β-triol on gene expression in irradiated BV2 cells

Project description:We aimed to study the potential role and underlying mechanism of 5α-androst-3β, 5α, 6β-triol on irradiated BV2 cells. We established radiation induced BV2 cells injury model and pretreated with 5α-androst-3β, 5α, 6β-triol or vehicle. We then performed gene expression profiling analysis using data obtained from RNA-seq of different groups.

2024-04-18 | GSE230636 | GEO

3β,6β-Diacet-oxy-5,9α-dihy-droxy-5α-cholest-7-en-11-one acetic acid 0.04-solvate.

Project description:The title compound, C31H48O7·0.04CH3COOH, is a polyoxy-genated steroid obtained by selective chemical oxidation of 7-de-hydro-cholesteryl acetate. The asymmetric unit comprises three mol-ecules of the steroid (Z' = 3) and a mol-ecule of acetic acid which has occupancy factor 0.131 (5). The geometric parameters of the independent mol-ecules do not reveal significant differences. In one mol-ecule, the terminal isopropyl group is disordered over two sets of sites with occupancy ratio 0.869 (5):0.131 (5). The three mol-ecules reveal different hydrogen-bonding patterns. Each of them is involved in an intra-molecular S(6) hydrogen-bonding motif, involving hy-droxy groups as donor and acceptor. In the crystal, two independent mol-ecules form dimers through hydrogen bonding between an OH donor and an acetate carbonyl acceptor, giving rise to R 2 (2)(16) ring patterns. A single hydrogen bond between the OH group and a ketone carbonyl group is observed between two symmetry-independent mol-ecules.

| S-EPMC3685037 | biostudies-literature

Neurosteroid allopregnanolone (3α,5α-THP) inhibits inflammatory signals induced by activated MyD88-dependent toll-like receptors.

Project description:We have shown that endogenous neurosteroids, including pregnenolone and 3α,5α-THP inhibit toll-like receptor 4 (TLR4) signal activation in mouse macrophages and the brain of alcohol-preferring (P) rat, which exhibits innate TLR4 signal activation. The current studies were designed to examine whether other activated TLR signals are similarly inhibited by 3α,5α-THP. We report that 3α,5α-THP inhibits selective agonist-mediated activation of TLR2 and TLR7, but not TLR3 signaling in the RAW246.7 macrophage cell line. The TLR4 and TLR7 signals are innately activated in the amygdala and NAc from P rat brains and inhibited by 3α,5α-THP. The TLR2 and TLR3 signals are not activated in P rat brain and they are not affected by 3α,5α-THP. Co-immunoprecipitation studies indicate that 3α,5α-THP inhibits the binding of MyD88 with TLR4 or TLR7 in P rat brain, but the levels of TLR4 co-precipitating with TRIF are not altered by 3α,5α-THP treatment. Collectively, the data indicate that 3α,5α-THP inhibits MyD88- but not TRIF-dependent TLR signal activation and the production of pro-inflammatory mediators through its ability to block TLR-MyD88 binding. These results have applicability to many conditions involving pro-inflammatory TLR activation of cytokines, chemokines, and interferons and support the use of 3α,5α-THP as a therapeutic for inflammatory disease.

| S-EPMC7909379 | biostudies-literature

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