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Usage

Uses

Used in Pharmaceutical Industry:
S-Mephenytoin is used as an anticonvulsant medication for the treatment of epilepsy, specifically to control seizures. Its ability to stabilize neural membranes and reduce the firing of excitatory neurons makes it an effective treatment option for individuals suffering from this neurological disorder.
Used in Neurology:
In the field of neurology, S-Mephenytoin is utilized as a therapeutic agent for managing epilepsy. Its mechanism of action involves stabilizing neural membranes and reducing the firing of excitatory neurons, which helps in controlling seizures and improving the quality of life for patients with epilepsy.

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 74-89-5 methylamine 
• 35373-92-3 L-phenylalanine methylamide 
• 501-53-1 benzyl chloroformate 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 

Downstream Products

• 1245640-65-6 C₂₀H₂₂N₂O₃ 
• 911289-30-0 C₁₆H₁₇N₃O₄*ClH 
• 911289-59-3 C₃₀H₂₉N₃O₄ 
• 97550-58-8 (S)-5-Benzyl-3-methyl-4-imidazolidinone hydrobromide 
• 120125-07-7 Boc-Tyr-D-Arg(NO₂)-Phe-NHCH₃ 
• 120125-06-6 Boc-D-Arg(NO₂)-Phe-NHCH₃ 
• 120124-87-0 Tyr-D-Arg-Phe-NHCH₃ 
• 264887-78-7 N-benzyloxycarbonyl-L-valyl-L-phenylalanine methylamide 
• 35373-92-3 L-phenylalanine methylamide 
• 97550-56-6 (S)-5-Benzyl-1-benzyloxycarbonyl-3-methyl-4-imidazolidinone 

Relevant academic research and scientific papers

A novel series of matrix metalloproteinase inhibitors for the treatment of inflammatory disorders

The preparation of a novel series of matrix metalloproteinase inhibitors is described, based on the use of a mercaptoacyl zinc binding moiety. The compounds have been tested in a model of rheumatoid arthritis and show good oral activity.

Synthesis, physical-chemical characterisation and biological evaluation of novel 2-amido-3-hydroxypyridin-4(1H)-ones: Iron chelators with the potential for treating Alzheimer's disease

A novel class of 2-amido-3-hydroxypyridin-4-one iron chelators is described. These compounds have been designed to behave as suitable molecular probes which will improve our knowledge of the role of iron in neurodegenerative conditions. Neurodegenerative disorders, such as Alzheimer's disease (AD) and Parkinson disease (PD), can be considered as diverse pathological conditions sharing critical metabolic processes such as protein aggregation and oxidative stress. Interestingly, both these metabolic alterations seem to be associated with the involvement of metal ions, including iron. Iron chelation is therefore a potential therapeutic approach. The physico-chemical (pKa, pFe 3+ and log P) and biological properties (inhibition of iron-containing enzymes) of these chelators have been investigated in order to obtain a suitable profile for the treatment of neurodegenerative conditions. Studies with neuronal cell cultures confirm that the new iron chelators are neuroprotective against β-amyloid-induced toxicity.

Enantioselective α-benzylation of aldehydes via photoredox organocatalysis

The first enantioselective aldehyde α-benzylation using electron-deficient aryl and heteroaryl substrates has been accomplished. The productive merger of a chiral imidazolidinone organocatalyst and a commercially available iridium photoredox catalyst in the presence of household fluorescent light directly affords the desired homobenzylic stereogenicity in good to excellent yield and enantioselectivity. The utility of this methodology has been demonstrated via rapid access to an enantioenriched drug target for angiogenesis suppression.

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.

OPTICAL ACTIVITY OF LACTONES AND LACTAMS-IV CHIROPTICAL PROPERTIES OF 4-IMIDAZOLIDINONES

The chiroptical properties of 4-imidazolidinones are reviewed.Several optically active compounds were obtained from amides and N-methylamides of corresponding N-acylamino acids.The origin of the two lowest energy electronic transitions is considered.The e