68388-08-9

Usage

General Description

2,5-Pyrrolidinedione, 1-[(2-chlorobenzoyl)oxy]- is a chemical compound also known as chlorphenesin carbamate. It is used as a muscle relaxant and topical antiseptic agent. It is commonly found in personal care products such as skin creams and lotions, where it is used as a preservative. This chemical works by inhibiting the release of acetylcholine at neuromuscular junctions, leading to muscle relaxation. It is considered non-toxic when used in small, regulated amounts in beauty and personal care products. However, excessive exposure to this chemical can cause irritation and sensitization. Therefore, it is important to use products containing chlorphenesin carbamate in moderation.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 118-91-2 ortho-chlorobenzoic acid 
• 17849-38-6 2-Chlorobenzyl alcohol 
• 89-98-5 2-chloro-benzaldehyde 

Downstream Products

• 142947-61-3 N,N'-bis<6-(2-chlorobenzamido)hexanoyl>cystamine 
• 142947-77-1 N,N'-bis<6-<(2-chlorobenzyl)amino>hex-1-yl>cystamine 
• 939794-52-2 5'-O-[N-(2-chlorobenzoyl)sulfamoyl]-2',3'-O-isopropylideneadenosine 
• 6392-26-3 (2-chlorophenyl)(morpholino)methanone 

Relevant academic research and scientific papers

An Engineered Aryl Acid Adenylation Domain with an Enlarged Substrate Binding Pocket

Adenylation (A) domains act as the gatekeepers of non-ribosomal peptide synthetases (NRPSs), ensuring the activation and thioesterification of the correct amino acid/aryl acid building blocks. Aryl acid building blocks are most commonly observed in iron-chelating siderophores, but are not limited to them. Very little is known about the reprogramming of aryl acid A-domains. We show that a single asparagine-to-glycine mutation in an aryl acid A-domain leads to an enzyme that tolerates a wide range of non-native aryl acids. The engineered catalyst is capable of activating non-native aryl acids functionalized with nitro, cyano, bromo, and iodo groups, even though no enzymatic activity of wild-type enzyme was observed toward these substrates. Co-crystal structures with non-hydrolysable aryl-AMP analogues revealed the origins of this expansion of substrate promiscuity, highlighting an enlargement of the substrate binding pocket of the enzyme. Our findings may be exploited to produce diversified aryl acid containing natural products and serve as a template for further directed evolution in combinatorial biosynthesis.

A photoinduced cross-dehydrogenative-coupling (CDC) reaction between aldehydes and N-hydroxyimides by a TiO2-Co ascorbic acid nanohybrid under visible light irradiation

In this study, we performed a visible light-mediated aerobic photo-cross dehydrogenative coupling (CDC) reaction between aldehydes and N-hydroxyimides using TiO2-AA-Co as a photocatalyst for the synthesis of active esters. The synergistic and selective effects of the cobalt ascorbic acid complex (Co-AA) and TiO2 nanoparticles on the visible-light photocatalytic activity were explored. The method possesses some advantages such as environmentally friendly conditions, easy work-up procedure, reusability, and scalability.

A copper-catalysed amidation of aldehydes via N-hydroxysuccinimide ester formation

A copper-catalysed oxidative amidation of aldehydes via N-hydroxysuccinimide ester formation is reported. The methodology employed to prepare amides directly from aldehydes has a very wide scope, is high yielding, and does not need dry conditions. This cross-coupling reaction appears to be simple and makes use of cheap, abundant and easily available reagents.

Iodide-catalyzed amide synthesis from alcohols and amines

An efficient method to prepare amides by a cascade strategy was developed. Using nBu4NI or NaI as the catalyst and tert-butyl hydroperoxide as the oxidant, various alcohols reacted with N-hydroxysuccinimide or N-hydroxyphthalimide affording corresponding active esters in moderate to good yield. The resulting active esters were converted into amides smoothly in one pot. The Royal Society of Chemistry 2013.

Organocatalytic amidation and esterification of aldehydes with activating reagents by a cross-coupling strategy

Formation on demand: An organocatalytic cross-coupling reaction of aldehydes with N-hydroxyimides, hexafluoroisopropyl alcohol, and sulfonimides has been developed. The resulting active intermediates can be directly converted into amides or esters in one pot. This simple method makes use of readily available starting materials, and the newly discovered activating reagents should find broad application in the synthesis of amides and esters. Copyright

5′-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: An adenylation enzyme required for siderophore biosynthesis of the mycobactins

A study of the structure - activity relationships of 5′-O-[N- (salicyl)sulfamoyl]adenosine (6), a potent inhibitor of the bifunctional enzyme salicyl-AMP ligase (MbtA, encoded by the gene Rv2384) in Mycobacterium tuberculosis, is described, targeting the salicyl moiety. A systematic series of analogues was prepared exploring the importance of substitution at the C-2 position revealing that a hydroxy group is required for optimal activity. Examination of a series of substituted salicyl derivatives indicated that substitution at C-4 was tolerated. Consequently, a series of analogues at this position provided 4-fluoro derivative, which displayed an impressive MIC 99 of 0.098 μM against whole-cell M. tuberculosis under iron-limiting conditions. Examination of other heterocyclic, cycloalkyl, alkyl, and aminoacyl replacements of the salicyl moiety demonstrated that these nonconserative modifications were poorly tolerated, a result consistent with the fairly strict substrate specificities of related non-ribosomal peptide synthetase adenylation enzymes.

N-hydroxysuccinimide-promoted oxidation of primary alcohols and aldehydes to form active esters with hypervalent(III) iodine

A simple, mild, and efficient method for the conversion of primary alcohols and aldehydes to N-hydroxysuccinimide esters with (diacetoxyiodo)benzene in high yield is developed. N-Hydroxysuccinimide acts not only as an esterification partner but also as an activator of PhI(OAc)2 in this reaction. Copyright

Benextramine-neuropeptide Y receptor interactions: Contribution of the benzylic moieties to [3H]neuropeptide Y displacement activity

Analogs of N,N'-bis[6-[(2-methoxybenzyl)amino]hex-1-yl]cystamine (benextramine, BXT, 2) were synthesized using solution-phase peptide synthesis methodology and analyzed for activity in displacing specifically bound 1 nM N-[propionyl-3H]neuropeptide Y([3H]NPY) from benextramine- sensitive neuropeptide Y (NPY) binding sites in rat brain. Our new synthetic approach to these analogs began with the acylation of cystamine with the N- hydroxysuccinimide ester of tert-butyloxycarbonyl (t-Boc) protected 6- aminohexanoic acid, followed by deprotection of the t-Boc groups with 4 N HCl in dioxane. Acylation of this symmetric diamine with N-hydroxysuccinimide esters of appropriately substituted benzoic acids, followed by reduction of the resultant tetraamides with diborane in refluxing THF, afforded the target compounds. The BXT analog lacking the benzylic group (i.e., compound 11) had no [3H]NPY displacement activity at concentrations up to 1.4 x 10-3 M. The 9-fold range in activities observed for the ortho, meta, and para regioisomers of the methoxy, chloro, and hydroxy benextramine analogs at benextramine-sensitive NPY rat brain binding sites does not differ from the range of potencies observed at α-adrenoceptors. However, the order of potencies at [3H]NPY sites differs from the order of potencies at α- adrenoceptors, with the m-methoxyphenyl (9a), m-hydroxyphenyl (10b), and 2- naphthyl (9f) analogs being the most active at [3H]NPY binding sites. The present results demonstrate the importance of the benzylic moiety for BXT's NPY antagonist activity, and suggest that the BXT binding site on the NPY receptor is significantly distinct from that on the α-adrenoceptor.