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Cystamine

Cystamine is an organic disulfide compound with the molecular formula C₄H₁₂N₂S₂ and the IUPAC name 2,2'-dithiodiethanamine, formed by the oxidative dimerization of cysteamine via a disulfide bond.^[1] It appears as a viscous, poisonous oil that is thermally unstable and decomposes upon distillation, so it is commonly handled as the more stable dihydrochloride salt.^[2] Discovered in 1907 during attempts to distill cystine and first synthesized in 1940 by oxidation of cysteamine with hydrogen peroxide, cystamine has found applications in chemical synthesis and materials science.^[2] It serves as a derivatizing agent for polymers in liquid chromatography analysis, a cross-linker for creating hydrogels, and a functionalizing agent for nanoparticles used in siRNA and DNA delivery systems.^[2] Biologically, cystamine demonstrates radioprotective and strong antioxidant properties, though its efficacy varies compared to its reduced form, cysteamine.^[3] It inhibits enzymes such as transglutaminase 2 and caspase-3, reduces protein aggregation, and upregulates neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and nuclear factor erythroid 2-related factor 2 (Nrf2) signaling.^[4] These mechanisms have positioned cystamine as a candidate for treating neurodegenerative diseases, including Huntington's disease, Parkinson's disease, Alzheimer's disease, and amyotrophic lateral sclerosis, with preclinical studies showing improved motor function, extended survival in disease models, and mitigation of oxidative stress and mitochondrial dysfunction.^[4] However, a subsequent phase II/III trial of cysteamine in HD patients did not demonstrate significant efficacy in slowing disease progression.^[5] Early clinical trials of cysteamine (the reduced form of cystamine), such as CYTE-I-HD for Huntington's disease, indicate tolerability despite gastrointestinal side effects.^[4] Additionally, cystamine reduces vascular stiffness in models of metabolic syndrome by inhibiting transglutaminase activity.^[6]

Properties

Chemical structure

Cystamine has the molecular formula C₄H₁₂N₂S₂ and the systematic name 2,2'-dithiobis(ethanamine).^[1]^[7] The molecule consists of a central disulfide bond (S-S) that connects two identical cysteamine units, each featuring a primary amine group (-NH₂) at the end of an ethyl chain.^[1] This structure can be textually represented as H₂N-CH₂-CH₂-S-S-CH₂-CH₂-NH₂.^[1] In comparison, cystamine differs from cystine by lacking the carboxylic acid groups present in the latter, as cystamine is the decarboxylated derivative of cystine.^[1] It also represents the oxidized, dimeric form of cysteamine, formed via oxidative coupling of the thiol groups in two cysteamine molecules.^[1] Cystamine is an achiral molecule, possessing no stereocenters due to its symmetric structure and lack of asymmetric carbon atoms.^[8]

Physical and chemical properties

Cystamine is typically supplied and handled as its dihydrochloride salt (C₄H₁₂N₂S₂·2HCl), which appears as a white to almost white crystalline powder or solid for enhanced stability.^[9] The free base form is an unstable, colorless to light yellow liquid with a density of approximately 1.09–1.12 g/cm³.^[10] The molecular weight of the free base is 152.28 g/mol, while the dihydrochloride salt has a molecular weight of 225.20 g/mol.^[1] The dihydrochloride salt exhibits a melting point of 214–222 °C, at which it decomposes.^[9] It demonstrates high solubility in water, exceeding 100 g/L (approximately 1 g/10 mL at room temperature), but shows low solubility in most organic solvents such as ethanol (around 2 mg/mL) and is practically insoluble in non-polar solvents like chloroform or ether.^[11] The free base is miscible with water and moderately soluble in ethanol.^[12] Chemically, cystamine features a disulfide bond that is susceptible to reduction by thiols or other reducing agents, yielding two molecules of cysteamine.^[13] The primary amine groups are basic, with a pKa value of approximately 9.91 for protonation.^[14] The compound remains stable under neutral aqueous conditions but can undergo hydrolysis or cleavage of the disulfide linkage in strong acidic or basic environments.^[15] In infrared (IR) spectroscopy, the characteristic S–S stretching vibration appears around 500 cm⁻¹. For ¹H NMR spectroscopy (in D₂O), the methylene protons adjacent to nitrogen (–CH₂–NH₂) resonate at approximately 3.42 ppm, while those adjacent to sulfur (–CH₂–S–) appear at about 3.05 ppm.^[16]

Synthesis

From cystine

Cystamine can be synthesized from cystine through thermal decarboxylation, a process in which the dicarboxylic amino acid undergoes heating to eliminate two molecules of carbon dioxide, yielding the diamine disulfide. The reaction proceeds as follows:

\text{HOOC-CH(NH}_2\text{)-CH}_2\text{-S-S-CH}_2\text{-CH(NH}_2\text{)-COOH} \rightarrow \text{H}_2\text{N-CH}_2\text{-CH}_2\text{-S-S-CH}_2\text{-CH}_2\text{-NH}_2 + 2 \text{CO}_2

This method requires an anhydrous environment to minimize side reactions and is typically conducted at high temperatures around 200–250 °C.^[17] The thermal decarboxylation of cystine was first reported in 1907 by Carl Neuberg and Edgar Ascher, who observed cystamine formation during dry distillation attempts on the amino acid.^[2] This historical approach remains a simple preparative route for small-scale laboratory production, leveraging cystine as a readily available natural precursor derived from proteins.^[18] Yields from dry distillation are generally low, often very small and accompanied by impurities due to the elevated temperatures involved, which can promote decomposition or unwanted byproducts.^[18] Despite these limitations, the method's straightforward nature—requiring no additional reagents—makes it suitable for basic synthetic needs, though purification steps are essential for obtaining usable cystamine.^[2]

From cysteamine

Cystamine is synthesized via the oxidative dimerization of cysteamine, in which the thiol groups of two cysteamine molecules (H₂N-CH₂-CH₂-SH) couple to form the disulfide linkage. This primary method employs mild oxidizing agents, including molecular oxygen, hydrogen peroxide, or iodine, to facilitate the reaction under controlled conditions.^[2]^[19]^[20] The reaction stoichiometry varies with the oxidant. For molecular oxygen, the process follows:

$2 \ \ce{H2N-CH2-CH2-SH} + \frac{1}{2} \ \ce{[O2](/page/The_O2)} \rightarrow \ce{H2N-CH2-CH2-S-S-CH2-CH2-NH2} + \ce{H2O}

This air oxidation proceeds readily in aqueous solution, particularly when catalyzed by transition metal ions.^[21] With hydrogen peroxide, the stoichiometry is:

$2 \ \ce{H2N-CH2-CH2-SH} + \ce{[H2O2](/page/Hydrogen_peroxide)} \rightarrow \ce{H2N-CH2-CH2-S-S-CH2-CH2-NH2} + 2 \ \ce{H2O}

The rate depends on the concentration of the thiolate anion, with optimal reactivity at mildly alkaline pH due to deprotonation of the thiol.^[20] For iodine, the reaction is:

\ce{I2 + 2 H2N-CH2-CH2-SH -> H2N-CH2-CH2-S-S-CH2-CH2-NH2 + 2 H+ + 2 I-}

This occurs via a bimolecular mechanism in neutral to mildly acidic media.^[19] These oxidations are conducted at mild temperatures, ranging from room temperature to 50 °C, and pH values adjusted based on the oxidant (typically 7–9 for many conditions) to minimize side reactions while promoting thiolate formation. Yields are high, often 80–90% or more, when oxygen is used with catalysts such as Cu²⁺ or Fe³⁺ ions, which accelerate the process by forming transient metal-thiolate complexes that enable electron transfer without radical intermediates.^[21]^[22]^[23] The copper-catalyzed variant, for instance, involves coordination of Cu(II) to two thiolate ligands, followed by intramolecular disulfide formation and reoxidation of Cu(I) by O₂.^[22] An alternative approach is electrochemical oxidation in aqueous media, where applied potential selectively oxidizes the thiol to the disulfide, offering precise control and avoiding chemical waste.^[24] This oxidative route from cysteamine supports pharmaceutical-grade production of cystamine, owing to its straightforward implementation and scalability for industrial applications.^[2]

Biological aspects

Metabolism

Cystamine is primarily metabolized through the intracellular reduction of its disulfide bond by the glutathione (GSH) system or thioredoxin, producing two molecules of cysteamine (H₂N-CH₂-CH₂-SH). This non-enzymatic reduction occurs rapidly in the reducing environment of the cytosol, where high GSH concentrations facilitate the process. The key reaction is represented as:

\text{cystamine} + 2 \text{GSH} \rightarrow 2 \text{cysteamine} + \text{GSSG}

where GSSG is glutathione disulfide. Liver and kidney tissues serve as the primary sites for this metabolism due to their high GSH levels and role in sulfur amino acid processing.^[25] Following reduction, cysteamine undergoes further oxidation to hypotaurine, catalyzed by the enzyme cysteamine dioxygenase (ADO), a thiol dioxygenase that incorporates molecular oxygen into the substrate. Hypotaurine is then converted to taurine through the action of sulfurtransferase enzymes, completing the metabolic pathway to this sulfonic acid, which is ultimately excreted in urine or incorporated into bile salts. This sequential transformation links cystamine metabolism to broader sulfur homeostasis and antioxidant defense mechanisms.^[25]^[26]^[27] Pharmacokinetically, cystamine demonstrates low oral bioavailability, primarily attributable to extensive first-pass metabolism in the liver, where rapid reduction to cysteamine occurs. Once in circulation, its plasma half-life is short, reflecting quick conversion and tissue distribution. These properties underscore the compound's dependence on cellular reducing systems for bioactivation and limit its systemic persistence.^[25]^[28]

Endogenous occurrence

Cystamine occurs endogenously primarily as the disulfide oxidation product of cysteamine, an aminothiol generated during the catabolism of coenzyme A via pantetheinase enzymes such as vanin-1 in mammalian cells.^[29] This minor biosynthetic pathway involves the oxidation of cysteamine, facilitated by molecular oxygen or transition metals, particularly under conditions of oxidative stress, or as an intermediate during the reduction of cystine.^[29] In eukaryotes, these cysteamine-derived pathways are evolutionarily conserved, underscoring their integral role in sulfur amino acid metabolism across diverse organisms.^[26] In mammalian tissues, cystamine is present at trace levels, notably in the brain, liver, gut, and lung, where it maintains low steady-state concentrations due to rapid reduction back to cysteamine in reducing cellular environments.^[29] Levels are generally submicromolar, reflecting its transient nature as a redox intermediate rather than a stable metabolite.^[30] For instance, cystamine has been shown to inactivate ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in vitro by promoting disulfide bond formation in the enzyme's active site.^[31] Physiologically, endogenous cystamine acts as a modulator of antioxidant defenses, participating in redox signaling by interacting with nitric oxide donors to form S-nitrosocysteamine and influencing nitrosative stress responses.^[29] It also contributes to cysteine homeostasis by depleting intracellular cystine pools, thereby regulating thiol-disulfide balance in cells.^[29] Quantification of cystamine in biological samples, such as tissues or fluids, requires methods sensitive to its instability and interconversion with cysteamine.

Applications and pharmacology

Therapeutic uses

Cystamine has been investigated as a prodrug to cysteamine for the treatment of nephropathic cystinosis, a lysosomal storage disorder characterized by cystine accumulation in cells. Upon oral administration, cystamine undergoes reduction in vivo to cysteamine, which facilitates disulfide exchange to deplete lysosomal cystine levels, thereby delaying renal failure and improving growth when initiated early. Cysteamine bitartrate remains the standard formulation due to better stability and tolerability, while cystamine derivatives, such as PEGylated forms, have been developed to enhance bioavailability and efficacy in preclinical models of cystinosis.^[32] In investigational applications, cystamine demonstrates neuroprotective effects in preclinical models of Huntington's disease (HD) through inhibition of tissue transglutaminase 2 (TG2), which reduces protein aggregation, and upregulation of brain-derived neurotrophic factor (BDNF), promoting neuronal survival and motor function improvement. Studies in R6/2 transgenic mice showed extended survival and ameliorated symptoms with cystamine doses of 10-20 mg/kg, though clinical translation has focused on cysteamine, with Phase II trials (e.g., CYTE-HD-01) yielding mixed results on efficacy despite good tolerability at 1.2 g/day delayed-release doses.^[33]^[34]^[35] For Alzheimer's disease, cystamine exhibits potential in reducing amyloid-beta aggregation via TG2 inhibition and antioxidant activity. Cysteamine has shown improvements in cognitive deficits in APP-Psen1 mouse models.^[4] Though human trials remain absent. In liver fibrosis models induced by carbon tetrachloride, cystamine attenuates fibrotic progression by suppressing collagen synthesis and oxidative stress, with intraperitoneal doses of 100 mg/kg reducing hepatic damage markers in rats. Historically, cystamine was included in the Soviet AI-2 emergency kit as a radioprotector against ionizing radiation, providing antioxidant shielding at doses of 0.2 g per tablet, though its use was discontinued after inconclusive trials in the 1960s-1970s.^[4]^[36]^[37] In a 2025 preclinical study, cystamine reduced neurodegeneration and epileptogenesis in a mouse model of Dravet syndrome.^[38] Administration of cystamine typically involves oral capsules at 1-2 g/day for therapeutic exploration, with good blood-brain barrier penetration supporting central nervous system applications. As of 2025, preclinical research continues into cystamine's role in neurodegenerative diseases, including nanoparticle formulations for targeted delivery to enhance solubility and reduce dosing frequency in cystinosis and fibrosis models.^[4]^[39]

Drug interactions and toxicity

Cystamine interacts with tubulin by binding to it, thereby inhibiting microtubule polymerization at millimolar concentrations and inducing abnormal tubulin aggregation.^[40] This interference disrupts cellular processes reliant on microtubule dynamics, such as mitosis and intracellular transport. Additionally, cystamine exhibits inherent anticoagulant activity by blocking fibrin crosslinking, inhibiting plasma clot formation, and reducing thrombin generation, which may potentiate the effects of existing anticoagulant therapies.^[41] Cystamine can also interfere with DNA-binding proteins through disulfide exchange reactions, potentially altering protein-nucleic acid interactions; this reactivity contributes to its radioprotective effects against ionizing radiation but raises concerns for mutagenic risks due to modification of critical sulfhydryl groups in regulatory proteins.^[42] The acute toxicity profile of cystamine includes an oral LD₅₀ of 896 mg/kg in rats and 874 mg/kg in mice, with an intraperitoneal LD₅₀ of 405 mg/kg in mice.^[43] Chronic exposure is associated with hepatotoxicity, manifesting as elevated liver enzymes and potential oxidative damage to hepatic tissue, alongside skin sensitization due to its thiol-like reactivity after reduction and gastrointestinal upset including nausea and vomiting.^[44] Adverse effects arise primarily from the disulfide moiety's reactivity, which promotes oxidative stress via disulfide interchange with cellular thiols, depleting antioxidants like glutathione and generating reactive oxygen species. At high doses, the amine groups may contribute to metabolic alkalosis by buffering cellular pH or interfering with acid-base homeostasis, though this effect is dose-dependent and less pronounced than direct oxidative damage.^[44] Cystamine's contraindications and monitoring requirements are analogous to those of cysteamine, including avoidance in pregnancy due to potential teratogenic effects observed in animal models with cysteamine, where it crosses the placenta and induces developmental abnormalities. Hypersensitivity reactions, including anaphylaxis, are also contraindications, and patients require monitoring of liver function tests during prolonged use to detect early hepatotoxicity.^[45]^[46] In cases of overdose, management focuses on supportive care, including gastrointestinal decontamination and symptomatic treatment for oxidative stress or alkalosis. N-acetylcysteine may be administered to replenish thiols and mitigate disulfide-induced oxidative damage, analogous to its role in countering related thiol toxicities.^[47]

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