37031-12-2

Usage

Uses

Given the provided materials, the specific uses of 4,5-dihydroxy-1,2-dithiane are not detailed extensively. However, based on its categorization and chemical structure, potential applications can be hypothesized in various industries:
Used in Pharmaceutical Industry:
4,5-Dihydroxy-1,2-dithiane could be used as a building block or intermediate in the synthesis of pharmaceutical compounds due to its unique structure and reactivity, potentially leading to the development of new drugs.
Used in Materials Science:
In materials science, 4,5-dihydroxy-1,2-dithiane might serve as a component in the development of novel materials owing to its sulfur-containing structure, which could influence the material's properties such as flexibility, stability, or reactivity.
Used in Biochemistry:
4,5-Dihydroxy-1,2-dithiane could be explored for its potential interactions with biological systems, possibly serving as a modifier or probe in biochemical research to understand its effects on biological molecules or processes.

InChI:InChI=1/C4H8O2S2/c5-3-1-7-8-2-4(3)6/h3-6H,1-2H2/t3-,4-/m1/s1

Upstream product

• 3483-12-3 DL-dithiothreitol 
• 97-72-3 2-Methylpropionic anhydride 
• 16096-98-3 trans-1,2-dithiane-4,5-diol 
• 27565-41-9 1,4-dithio-D,L-threitol 
• 1077-28-7 Thioctic acid 
• 1892-29-1 bis(2-hydroxyethyl) disulfide 
• 131760-68-4 1,2-dimethyl-3,8-dioxo-1,2,5,6-diazadithiocane 
• 27025-41-8 glutathione disulfide 
• 145626-93-3 Bis(2-mercaptoethyl) Sulfone Disulfide 
• 145627-07-2 1,2-Bis(mercaptomethyl)-4-methylurazole Disulfide 
• 145626-99-9 N,N'-Bis(2-mercaptoacetyl)hexahydropyridazine Disulfide 
• 145626-94-4 N,N'-Dicarbomethoxy-N,N'-bis(mercaptomethyl)ethylenediamine Disulfide 
• 145627-03-8 N,N'-Dicarbethoxy-N,N'-bis(mercaptomethyl)hydrazine Disulfide 
• 62671-38-9 bis (1-methyl-(1H)-tetrazol-5-yl)-disulfide 

Downstream Products

• 27565-41-9 1,4-dithio-D,L-threitol 
• 683278-62-8 trans-2,3-dihydroxy-1-mercaptotetrahydrothiophene 

Relevant academic research and scientific papers

Seleno-Michael Reaction of Stable Functionalised Alkyl Selenols: A Versatile Tool for the Synthesis of Acyclic and Cyclic Unsymmetrical Alkyl and Vinyl Selenides

Seleno-Michael additions of stable functionalised primary alkyl selenols to activated alkenes and alkynes are described. In the presence of Al2O3, β-hydroxy-, β-amino-, and β-mercapto selenols react smoothly with electron-poor alkenes and alkynes to afford the corresponding unsymmetrical functionalised dialkyl- and alkyl?vinyl-selenides in good yield. The very mild conditions allow a broad range of selenols and Michael acceptors to be converted into the corresponding synthetically valuable seleno-Michael adducts, demonstrating high selectivity and excellent functional group tolerance. Hydroxy- and mercapto-substituted vinyl selenides were efficiently employed for the synthesis of functionalised 1,3-oxaselenolanes, 1,3-thiaselenolanes, and 1,4-thiaselenanes through intramolecular oxa- and thia-Michael additions. Furthermore, a NaH-promoted lactonization enables the synthesis of variously substituted 2-oxo-1,4-oxaselenanes from hydroxy?vinyl-selenides. Evaluation of thiol peroxidase-like properties of novel functionalised organoselenides demonstrated that they possess a remarkable catalytic antioxidant activity. (Figure presented.).

Modeling Thioredoxin Reductase-Like Activity with Cyclic Selenenyl Sulfides: Participation of an NH???Se Hydrogen Bond through Stabilization of the Mixed Se?S Intermediate

At the redox-active center of thioredoxin reductase (TrxR), a selenenyl sulfide (Se?S) bond is formed between Cys497 and Sec498, which is activated into the thiolselenolate state ([SH,Se?]) by reacting with a nearby dithiol motif ([SHCys59,SHCys64]) present in the other subunit. This process is achieved through two reversible steps: an attack of a cysteinyl thiol of Cys59 at the Se atom of the Se?S bond and a subsequent attack of a remaining thiol at the S atom of the generated mixed Se?S intermediate. However, it is not clear how the kinetically unfavorable second step progresses smoothly in the catalytic cycle. A model study that used synthetic selenenyl sulfides, which mimic the active site structure of human TrxR comprising Cys497, Sec498, and His472, suggested that His472 can play a key role by forming a hydrogen bond with the Se atom of the mixed Se?S intermediate to facilitate the second step. In addition, the selenenyl sulfides exhibited a defensive ability against H2O2-induced oxidative stress in cultured cells, which suggests the possibility for medicinal applications to control the redox balance in cells.

Efficient resolution of oxidized Cleland's reagent by C2-symmetric BOC- L-phenylalanyl esters

Trans 4,5-dihydroxy-1,2-dithiane (1,oxidized form of Cleland's reagent; dithiothreitol) is resolved efficiently in > 99% overall e.e. into its two enantiomers by fractional recrystallization of its BOC-L-phenylalanyl diesters.

Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif

Specialized cellular networks of oxidoreductases coordinate the dithiol/disulfide-exchange reactions that control metabolism, protein regulation, and redox homeostasis. For probes to be selective for redox enzymes and effector proteins (nM to μM concentrations), they must also be able to resist non-specific triggering by the ca. 50 mM background of non-catalytic cellular monothiols. However, no such selective reduction-sensing systems have yet been established. Here, we used rational structural design to independently vary thermodynamic and kinetic aspects of disulfide stability, creating a series of unusual disulfide reduction trigger units designed for stability to monothiols. We integrated the motifs into modular series of fluorogenic probes that release and activate an arbitrary chemical cargo upon reduction, and compared their performance to that of the literature-known disulfides. The probes were comprehensively screened for biological stability and selectivity against a range of redox effector proteins and enzymes. This design process delivered the first disulfide probes with excellent stability to monothiols yet high selectivity for the key redox-Active protein effector, thioredoxin. We anticipate that further applications of these novel disulfide triggers will deliver unique probes targeting cellular thioredoxins. We also anticipate that further tuning following this design paradigm will enable redox probes for other important dithiol-manifold redox proteins, that will be useful in revealing the hitherto hidden dynamics of endogenous cellular redox systems.

Click Reaction of Selenols with Isocyanates: Rapid Access to Selenocarbamates as Peroxide-Switchable Reservoir of Thiol-Peroxidase-Like Catalysts

Selenols react with isocyanates under mild catalyst-free conditions to generate selenocarbamates in good yield and with high selectivity over potentially competing nucleophilic additions. The methodology enables the incorporation of a wide variety of functional groups providing access to a broad array of densely functionalised selenocarbamates. In the presence of competing heteroatom-centered nucleophiles, isocyanates selectively couple with selenols. Selenocarbamates exhibited thiol-peroxidase-like properties, enabling the reduction of hydrogen peroxide at the expense of thiols, which are converted into the corresponding disulfides. A series of control experiments suggested that the catalytic mechanism proceeds through a pathway, involving a H2O2-promoted transcarbamoylation reaction leading to a thiocarbamate with concomitant releasing of catalytically active selenolate anions. By undergoing peroxide-driven thiol-selenol exchange, selenocarbamates behave as equivalents of selenolate anions with thiol-peroxidase-like activity. (Figure presented.).

Oxidative Formation of Disulfide Bonds by a Chemiluminescent 1,2-Dioxetane under Mild Conditions

The oxidation of alkyl thiols to disulfides has been achieved under mild conditions using a chemiluminescent 1,2-dioxetane as a stoichiometric oxidant. Besides the mild and biocompatible reaction conditions, this approach offers the possibility to monitor the presence of thiols through oxidation and chemiluminescence of the remaining dioxetane.

Disulfide-Unit Conjugation Enables Ultrafast Cytosolic Internalization of Antisense DNA and siRNA

Development of intracellular delivery methods for antisense DNA and siRNA is important. Previously reported methods using liposomes or receptor-ligands take several hours or more to deliver oligonucleotides to the cytoplasm due to their retention in endosomes. Oligonucleotides modified with low molecular weight disulfide units at a terminus reach the cytoplasm 10 minutes after administration to cultured cells. This rapid cytoplasmic internalization of disulfide-modified oligonucleotides suggests the existence of an uptake pathway other than endocytosis. Mechanistic analysis revealed that the modified oligonucleotides are efficiently internalized into the cytoplasm through disulfide exchange reactions with the thiol groups on the cellular surface. This approach solves several critical problems with the currently available methods for enhancing cellular uptake of oligonucleotides and may be an effective approach in the medicinal application of antisense DNA and siRNA.

1,2-DITHIOLANE COMPOUNDS USEFUL IN NEUROPROTECTION, AUTOIMMUNE AND CANCER DISEASES AND CONDITIONS

This invention provides confounds of the formula (I): wherein Y1, Y2 Z, X1, X2, and W are defined in the specification. These compounds are useful in the treatment of tyrosine kinases, MAPK signaling pathway kinases and Ρ13K/ΑΚΤ/mTor signaling pathway kinases-mediated diseases; or conditions, such as neurodegeneration, neuroprotection, cancer, autoimmune as well as other diseases and conditions associated with the modulation of tyrosine kinases selected from FYN, FYN Y531F, FLT3, FLT3 -ITD, BRK, ITK, FRK, BTK, BMX, SRC, FGR, YES1, LCK, HCK, RET, CSK, LYN, and ROSI; MAPK pathway kinases selected from ARAF, BRAE CRAP, ERK1 /2, MEK1, MEK2, MEK3, MEK4, MEK5. MEK6, and MEK7; and P13K/AKT/mTor pathway kinases: selected from mTor, P13K a, Ρ13Κ β, P13Kγ, and P13K δ.

Syntheses of prodrug-type phosphotriester oligonucleotides responsive to intracellular reducing environment for improvement of cell membrane permeability and nuclease resistance

We synthesized prodrug-type phosphotriester (PTE) oligonucleotides containing the six-membered cyclic disulfide moiety by using phosphoramidite chemistry. Prodrug-type oligonucleotides named “Reducing-Environment-Dependent Uncatalyzed Chemical Transforming (REDUCT) PTE oligonucleotides” were converted into natural oligonucleotides under cytosol-mimetic reductive condition. Furthermore, the REDUCT PTE oligonucleotides were robust to nuclease digestion and exhibited good cell membrane permeability.

Hydrogen Bonding-Assisted Enhancement of the Reaction Rate and Selectivity in the Kinetic Resolution of d,l-1,2-Diols with Chiral Nucleophilic Catalysts

An extremely efficient acylative kinetic resolution of d,l-1,2-diols in the presence of only 0.5 mol% of binaphthyl-based chiral N,N-4-dimethylaminopyridine was developed (selectivity factor of up to 180). Several key experiments revealed that hydrogen bonding between the tert-alcohol unit(s) of the catalyst and the 1,2-diol unit of the substrate is critical for accelerating the rate of monoacylation and achieving high enantioselectivity. This catalytic system can be applied to a wide range of substrates involving racemic acyclic and cyclic 1,2-diols with high selectivity factors. The kinetic resolution of d,l-hydrobenzoin and trans-1,2-cyclohexanediol on a multigram scale (10 g) also proceeded with high selectivity and under moderate reaction conditions: (i) very low catalyst loading (0.1 mol%); (ii) an easily achievable low reaction temperature (0 °C); (iii) high substrate concentration (1.0 M); and (iv) short reaction time (30 min). (Figure presented.).