83708-38-7

Usage

Molecular Weight

Not provided in the material

Chemical Class

Isoindole-1,3-diones

Structural Feature

A phenoxypropyl group attached to the 2-position of the isoindole ring system

Potential Applications

Pharmaceutical and organic synthesis

Properties

Interesting properties due to the presence of the isoindole ring

Research Prospects

Promising candidate for further research and development in various chemical and biological applications

Upstream product

• 85-44-9 phthalic anhydride 
• 412297-67-7 N,N'-bis-(3-phenoxy-propyl)-urea 
• 42251-84-3 N-(3-chloropropyl)phthalimide 
• 108-95-2 phenol 
• 1074-82-4 potassium phtalimide 
• 588-63-6 3-phenoxypropyl bromide 
• 524-38-9 N-hydroxyphthalimide 
• 5460-29-7 2-(3-bromopropyl)isoindole-1,3-dione 
• 136918-14-4 phthalimide 
• 139-02-6 sodium phenoxide 

Downstream Products

• 7617-76-7 3-phenoxypropanamine 
• 1350730-42-5 C₂₈H₂₇N₂O₄⁽¹⁺⁾*Cl^(1-) 
• 98510-48-6 2-amino-5-nitroso-6-(3-phenoxypropyl)aminopyrimidin-4(3H)-one 
• 865086-04-0 N-(3-phenoxypropyl)-isoindoline 
• 865086-17-5 C₁₇H₁₅⁽²⁾H₄NO 

Relevant academic research and scientific papers

Photochemical Decarboxylative C(sp3)-X Coupling Facilitated by Weak Interaction of N-Heterocyclic Carbene

While N-hydroxyphthalimide (NHPI) ester has emerged as a powerful reagent as an alkyl radical source for a variety of C-C bond formations, the corresponding C(sp3)-N bond formation is still in its infancy. We demonstrate herein transition-metal-free decarboxylative C(sp3)-X bond formation enabled by the photochemical activity of the NHPI ester-NaI-NHC complex, giving primary C(sp3)-(N)phth, secondary C(sp3)-I, or tertiary C(sp3)-(meta C)phth coupling products. The primary C(sp3)-(N)phth coupling offers convenient access to primary amines.

Discovery of N-Aryloxypropylbenzylamines as Voltage-Gated Sodium Channel NaV1.2-Subtype-Selective Inhibitors

We previously reported that a lipophilic N-(4′-hydroxy-3′,5′-di-tert-butylbenzyl) derivative (1) of the voltage-gated sodium channel blocker mexiletine, was a more potent sodium channel blocker in vitro and in vivo. We demonstrate that replacing the chiral methylethylene linker between the amine and di-tert-butylphenol with an achiral 1,3-propylene linker (to give (2)) maintains potency in vitro. We synthesized 25 analogues bearing the 1,3-propylene linker and found that minor structural changes resulted in pronounced changes in state dependence of blocking human NaV1.2 and 1.6 channels by high-throughput patch-clamp analysis. Compared to mexiletine, compounds 1 and 2 are highly selective NaV1.2 inhibitors and >500 times less potent in inhibiting NaV1.6 channels. On the other hand, a derivative (compound 4) bearing 2,6-dimethoxy groups in place of the 2,6-dimethyl groups found in mexiletine was found to be the most potent inhibitor, but is nonselective against both channels in the tonic, frequency-dependent and inactivated states. In a kindled mouse model of refractory epilepsy, compound 2 inhibited seizures induced by 6 Hz 44 mA electrical stimulation with an IC50 value of 49.9±1.6 mg kg?1. As established sodium channel blockers do not suppress seizures in this mouse model, this indicates that 2 could be a promising candidate for treating pharmaco-resistant epilepsy.

Photoinduced, Copper-Catalyzed Decarboxylative C-N Coupling to Generate Protected Amines: An Alternative to the Curtius Rearrangement

The Curtius rearrangement is a classic, powerful method for converting carboxylic acids into protected amines, but its widespread use is impeded by safety issues (the need to handle azides). We have developed an alternative to the Curtius rearrangement that employs a copper catalyst in combination with blue-LED irradiation to achieve the decarboxylative coupling of aliphatic carboxylic acid derivatives (specifically, readily available N-hydroxyphthalimide esters) to afford protected amines under mild conditions. This C-N bond-forming process is compatible with a wide array of functional groups, including an alcohol, aldehyde, epoxide, indole, nitroalkane, and sulfide. Control reactions and mechanistic studies are consistent with the hypothesis that copper species are engaged in both the photochemistry and the key bond-forming step, which occurs through out-of-cage coupling of an alkyl radical.

Synthesis, biological evaluation of 9-N-substituted berberine derivatives as multi-functional agents of antioxidant, inhibitors of acetylcholinesterase, butyrylcholinesterase and amyloid-β aggregation

A series of 9-N-substituted berberine derivatives were synthesized and biologically evaluated as antioxidant and inhibitors of acetylcholinesterase (AChE), butyrylcholinesterase and amyloid-β aggregation. Most of these compounds exhibited very good antioxidant activities, inhibitive activities of AChE and amyloid-β aggregation. Among them, compound 8d, (o-methylphenethyl)amino linked at the 9-position of berberine, was found to be a good antioxidant (with 4.05 μM of Trolox equivalents), potent inhibitor of AChE (an IC50 value of 0.027 μM), and high active inhibitor of amyloid-β aggregation (an IC50 value of 2.73 μM).

Inhibitors of protein tyrosine phosphatase

The present invention comprises small molecular weight, non-peptidic inhibitors of formulae I-VII of Protein Tyrosine Phosphatase 1 (PTP1) which are useful for the treatment and/or prevention of Non-Insulin Dependent Diabetes Mellitus (NIDDM).

Pyridazinone derivatives and processes for preparing the same

Disclosed is a pyridazinone compound represented by the formula (I): STR1 wherein X represents hydrogen atom or the like; Y represents a single bonding arm, oxygen atom or sulfur atom; A represents a straight or branched alkylene group which may have a double bond; B represents carbonyl group or thiocarbonyl group; and R2 represents an alkyl group having 1 to 10 carbon atoms which may be substituted or the like; or B represents sulfonyl group; and R2 represents a lower alkenyl group or the like; R1 represents hydrogen atom or the like; R3 represents hydrogen atom or the like; R4 represents hydrogen atom or the like; and R5 represents hydrogen atom or the like, or a pharmaceutically acceptable salt thereof.

Monocyclic Pteridine Analogues. Inhibition of Escherichia coli Dihydropteroate Synthase by 6-Amino-5-nitrosoisocytosines

A variety of 5,6-disubstituted isocytosine derivatives were evaluated in vitro as inhibitors of dihydropteroate synthase from Escherichia coli.A number of 6-(alkylamino)-5-nitrosoisocytosines have in vitro potency equivalent with or superior to that of therapeutically effective sulfonamide inhibitors of the synthase.The sulfonamide drugs are known to complete for the p-aminobenzoic acid binding site of the synthase, and kinetic analysis of inhibition of the synthase by 6-(methylamino)-5-nitrosoisocytosine (16; I50 = 1.6 μM) and by the 6-(3-phenoxypropyl)amino analogue (33; I50 = 3.7 μM) indicated that the nitrosoisocytosine inhibitors compete with the pteridine substrate for the enzyme.Structure-activity studies demonstrated that the enzyme surface has a low tolerance for steric bulk in the region surrounding the isocytosine 6-amino function.However, this steric intolerance may be counterbalanced to a significant degree by positive allosteric interactions achieved by certain analogues that have a 6-(ω-phenylalkyl)amino substituent.For example, 6--5-nitrosoisocytosine (28) is as effective an inhibitor (I50 = 1.4 μM) as the 6-methylamino compound 16.Although several members of the 5-nitroso series were potent synthase inhibitors, none of the nitrosoisocytosines exhibited significant antibacterial activity.This observation may reflect poor transport of these compounds through the bacterial cell wall or, alternatively, may result from a rapid metabolic inactivation process.