487-58-1

Basic information

• Product Name: lenticin
• Synonyms: lenticin;N,N,N-Trimethyl-1-carboxylato-2-(1H-indole-3-yl)ethanaminium;α-Carboxylato-N,N,N-trimethyl-1H-indole-3-ethan-1-aminium;tryptophan betaine;(1-Carboxy-2-indol-3-ylethyl)trimethylammonium hydroxide inner salt;Glyyunnanenine;Lenticine;L-Hypaphorine
• CAS NO: 487-58-1
• Molecular Formula: C₁₄H₁₈N₂O₂
• Molecular Weight: 246.30492
• Mol File: 487-58-1.mol
• Article Data: 6

Chemical Properties

• Melting Point: 255℃ (decomposition)
• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: g/cm³
• Storage Temp.: -20°C
• CAS DataBase Reference: lenticin(CAS DataBase Reference)
• NIST Chemistry Reference: lenticin(487-58-1)
• EPA Substance Registry System: lenticin(487-58-1)

Safety Data

• Hazard Codes: Xn,N
• Statements: 22-50
• Safety Statements: 61
• Hazardous Substances Data: 487-58-1(Hazardous Substances Data)

Usage

Description

Lenticin is an amino acid betaine derived from the exhaustive methylation of the alpha-amino group of L-tryptophan, with the concurrent deprotonation of the carboxy group. It is a unique compound with potential applications in various industries due to its specific chemical properties.

Uses

Used in Pharmaceutical Industry:
Lenticin is used as a pharmaceutical compound for its potential therapeutic effects. The exhaustive methylation and deprotonation processes involved in its synthesis may contribute to its ability to interact with biological systems, making it a candidate for further research and development in the medical field.
Used in Chemical Research:
Lenticin can be utilized as a research tool in chemical and biochemical studies. Its unique structure and properties may provide insights into the behavior of amino acid betaines and their interactions with other molecules, furthering our understanding of biochemistry and potentially leading to new discoveries.
Used in Material Science:
The specific chemical properties of lenticin, such as its methylation and deprotonation, may make it a valuable component in the development of new materials with unique characteristics. It could be used as a building block or modifier in the creation of novel materials with specific properties for various applications.
Used in Cosmetics Industry:
Lenticin's unique structure and properties may also find applications in the cosmetics industry. It could potentially be used as an active ingredient in skincare products, where its interactions with biological systems could provide benefits such as anti-aging, skin repair, or other therapeutic effects.

InChI:InChI=1/C14H18N2O2/c1-16(2,3)13(14(17)18)8-10-9-15-12-7-5-4-6-11(10)12/h4-7,9,13,15H,8H2,1-3H3/t13-/m1/s1

Upstream product

• 485-80-3 S-adenosyl-L-methionine 
• 73-22-3 L-Tryptophan 
• 526-31-8 L-abrine 
• 74-88-4 methyl iodide 
• 54648-79-2 O-Methyl-N,N'-diisopropylisourea 

Downstream Products

• 120-72-9 indole 
• 75-50-3 trimethylamine 

Relevant articles and documents

L-Hypaphorine and D-hypaphorine: Specific antiacetylcholinesterase activity in rat brain tissue

Acetylcholinesterase (AChEis) inhibitors are used to treat neurodegenerative diseases like Alzheimer's disease (AD). L-Hypaphorine (L-HYP) is a natural indole alkaloid that has been shown to have effects on the central nervous system (CNS). The goal of this research was to synthesize L-HYP and D-HYP and test their anticholinesterasic properties in rat brain regions. L-HYP suppressed acetylcholinesterase (AChE) activity only in the cerebellum, whereas D-HYP inhibited AChE activity in all CNS regions studied. No cytotoxic effect on normal human cells (HaCaT) was observed in the case of L-HYP and D-HYP although an increase in cell proliferation. Molecular modeling studies revealed that D-HYP and L-HYP have significant differences in their binding mode positions and interact stereospecifically with AChE's amino acid residues.

Ergothioneine biosynthetic methyltransferase EgtD reveals the structural basis of aromatic amino acid betaine biosynthesis

Ergothioneine is an N-α-trimethyl-2-thiohistidine derivative that occurs in human, plant, fungal, and bacterial cells. Biosynthesis of this redox-active betaine starts with trimethylation of the α-amino group of histidine. The three consecutive methyl transfers are catalyzed by the S-adenosylmethionine-dependent methyltransferase EgtD. Three crystal structures of this enzyme in the absence and in the presence of N-α-dimethylhistidineand S-adenosylhomocysteine implicate a preorganized array of hydrophilic interactions as the determinants for substrate specificity and apparent processivity. We identified two active site mutations that change the substrate specificity of EgtD 107-fold and transform the histidine-methyltransferase into a proficient tryptophan-methyltransferase. Finally, a genomic search for EgtD homologues in fungal genomes revealed tyrosine and tryptophan trimethylation activity as a frequent trait in ascomycetous and basidomycetous fungi.

Betaines derived from amino and hydrazino acids as phase transfer catalysts

Betaines derived from α-, β- and γ-amino acids (obtained by alkylation of the corresponding amino acids with O-methyl-N.N'- diisopropylisourea) as well as β-hydrazino acids (prepared by dehydrohalogenative hydrolysis of methyl 3-(2-alkyl-2,2-dimethylhydra