6909-65-5

Usage

Heterocyclic compound

The compound contains a heterocyclic ring, which is a ring structure containing at least one atom that is not carbon, in this case, the thiophene ring.

Thiophene ring

The compound contains a five-membered ring with a sulfur atom as one of the members, which is a characteristic feature of thiophene.

Bromine substituent

The thiophene ring has a bromine atom attached to it, which can be used for various applications in organic synthesis and medicinal chemistry.

Dioxolane ring

The compound contains a five-membered ring with two oxygen atoms as two of the members, which is a characteristic feature of dioxolane.

Methyl group

The dioxolane ring has a methyl group attached to it, which can be used as a building block in organic synthesis.

Building block in organic synthesis

The compound is often used as a building block in organic synthesis due to its unique structure and reactivity.

Medicinal chemistry

The compound is used in medicinal chemistry, particularly in the synthesis of pharmaceuticals.

Reagent in the synthesis of pharmaceuticals and agrochemicals

The bromine substituent on the thiophene ring makes 2-(5-bromothiophen-2-yl)-2-methyl-1,3-dioxolane useful as a reagent in the synthesis of pharmaceuticals and agrochemicals.

Potential pharmacological and biological activities

The unique structure and reactivity of the compound make it a valuable tool in the development of new compounds with potential pharmacological and biological activities.

Upstream product

• 5370-25-2 2-Acetyl-5-bromothiophene 
• 107-21-1 ethylene glycol 

Downstream Products

• 18494-73-0 5,5'-di(1-oxoethyl)-2,2'-bithiophene 

Relevant academic research and scientific papers

CYCLIC SULFAMIDE COMPOUNDS AND METHODS OF USING SAME

The present disclosure provides, in part, cyclic sulfamide compounds, and pharmaceutical compositions thereof, useful as modulators of Hepatitis B (HBV) core protein, and methods of treating Hepatitis B (HBV) infection.

Molecular recognition at the active site of factor Xa: Cation-π Interactions, stacking on planar peptide surfaces, and replacement of structural water

Factor Xa, a serine protease from the blood coagulation cascade, is an ideal enzyme for molecular recognition studies, as its active site is highly shape-persistent and features distinct, concave sub-pockets. We developed a family of non-peptidic, small-molecule inhibitors with a central tricyclic core orienting a neutral heterocyclic substituent into the S1 pocket and a quaternary ammonium ion into the aromatic box in the S4 pocket. The substituents were systematically varied to investigate cation-π interactions in the S4 pocket, optimal heterocyclic stacking on the flat peptide walls lining the S1 pocket, and potential water replacements in both the S1 and the S4 pockets. Structure-activity relationships were established to reveal and quantify contributions to the binding free enthalpy, resulting from single-atom replacements or positional changes in the ligands. A series of high-affinity ligands with inhibitory constants down to Ki=2nM were obtained and their proposed binding geometries confirmed by X-ray co-crystal structures of protein-ligand complexes. Factor Xa is an ideal enzyme to undertake molecular recognition studies at atomic level resolution as its active site is completely conserved in complexes with designed ligands. Cation-π interactions, water replacements, and stacking interactions with flat peptide fragments were investigated, revealing large changes in binding affinity resulting from single-atom mutations or positional shifts of heteroatoms in the ligands. Copyright

Pharmacological agents and methods of treatment that inactivate pathogenic prokaryotic and eukaryotic cells and viruses by attacking highly conserved domains in structural metalloprotein and metalloenzyme targets

The invention relates to the treatment of viral, bacterial, parasitic, proliferative diseases, neurodegenerative diseases, inflammatory diseases, immunological diseases, transplanted organ rejection, and diseases produced by intoxication with heavy metals. The invention relates to the use of specific metal chelating agents including, furoic acid, 2-thiophenecarboxylic acid and their derivatives, analogs and structurally related chemicals as pharmacological agents that can be used effectively to disrupt and inactivate specific transition metal ion containing zinc finger structural motifs in metalloproteins and specific transition metal ion containing catalytic sites in metalloproteinases, which in turn, inactivate the pathogenic virus, pathogenic prokaryotic or eukaryotic cells which produces disease conditions. The preparations can be administered topically or for systemic use. The preparations are novel wide-spectrum antibiotics which have antiviral, antiproliferative, antineoplastic, antiangiogenic, antibacterial, antiparasitic, antiinfective, and anti-inflammatory effects and can be used in the treatment and prevention of diseases such as AIDS, cancers, untoward angiogenesis, pulmonary anthrax, malaria, inflammatory responses, Alzheimer's disease and other diseases.

A Convenient Synthetic Route to bis-Heteroaromatic and bis-Heterocyclic Compounds Promoted by Liganded Nickel Complex Reducing Agents.

A number of nitrogen, sulfur or oxygen containing bis-heteroaromatic or bis-heterocyclic derivatives have been synthesized in good to excellent yields by homocoupling of the corresponding halogenated compounds in the presence of liganded (triphenylphosphine or 2,2'-bipyridine) nickel Complex Reducing Agents in THF or DME at 63 deg C.