64987-81-1

Basic information

• Product Name: 4-(2-N-Maleimido)methyl benzoic acid
• Synonyms: 4-(2-N-Maleimido)methyl benzoic acid;Benzoic acid, 4-[(2,5-dihydro-2,5-dioxo-1H-pyrrol-1-yl)Methyl]-
• CAS NO: 64987-81-1
• Molecular Formula: C₁₂H₉NO₄
• Molecular Weight: 231.20416
• Mol File: 64987-81-1.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 464.8±38.0 °C(Predicted)
• Appearance: /
• Density: 1.473±0.06 g/cm3(Predicted)
• PKA: 4.15±0.10(Predicted)
• CAS DataBase Reference: 4-(2-N-Maleimido)methyl benzoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 4-(2-N-Maleimido)methyl benzoic acid(64987-81-1)
• EPA Substance Registry System: 4-(2-N-Maleimido)methyl benzoic acid(64987-81-1)

Safety Data

• Hazardous Substances Data: 64987-81-1(Hazardous Substances Data)

Usage

General Description

4-(2-N-Maleimido)methyl benzoic acid is a chemical compound that is used in various research and medicinal applications. It is a derivative of benzoic acid with a maleimide group attached to the N-atom. 4-(2-N-Maleimido)methyl benzoic acid is commonly used in the development of targeted drug delivery systems, as the maleimide group can react with thiol groups on proteins, allowing for specific targeting of the drug to certain cells or tissues. It is also used in the conjugation of proteins and peptides for various biochemical and analytical techniques. Additionally, it can be used in the synthesis of various organic compounds for research purposes.

Upstream product

• 150-13-0 4-amino-benzoic acid 
• 904791-14-6 4-[(3-carboxy acryloylamino)methyl]benzoic acid 
• 56-91-7 p-aminomethylbenzoic acid 

Downstream Products

• 1089724-91-3 4-(2,5-dioxo-2,5-dihydropyrrol-1-ylmethyl)-N-[4-methyl-3-(4-pyridin-3-yl-pyrimidin-2-ylamino)-phenyl]benzamide 

Relevant articles and documents

LIQUID CRYSTAL THERMOSET MONOMER OR OLIGOMER, THERMOSETTING LIQUID CRYSTAL POLYMER COMPOSITION COMPRISING THE SAME AND PRINTED CIRCUIT BOARD USING THE SAME

A liquid crystal thermoset (LCT) monomer or oligomer having both ends capped with maleimide having at least one methyl group, represented by Formula 1: wherein R1 and R2 are each independently CH3 or H, and at least one of

Design, synthesis, and biochemical evaluation of N-substituted maleimides as inhibitors of prostaglandin endoperoxide synthases

N-(Carboxyalkyl)maleimides are rapid as well as time-dependent inhibitors of prostaglandin endoperoxide synthase (PGHS). The corresponding N- alkylmaleimides were only time-dependent inactivators of PGHS, suggesting that the carboxylate is critical for rapid inhibition. Several N-substituted maleimide analogs containing structural features similar to those of the nonsteroidal anti-inflammatory drug aspirin were synthesized and evaluated as inhibitors of PGHS. Most of the aspirin-like maleimides inactivated the cyclooxygenase activity of purified ovine PGHS-1 in a time- and concentration-dependent manner similar to that of aspirin. The peroxidase activity of PGHS was also inactivated by the maleimide analogs. The cyclooxygenase activity of the inducible isozyme, i.e., PGHS-2, was also inhibited by these compounds. The corresponding succinimide analog of N-5- maleimido-2-acetoxy-1-benzoic acid did not inhibit either enzyme activity, suggesting that inactivation was due to covalent modification of the protein. The mechanism of inhibition of PGHS-1 by N-(carboxyheptyl)maleimide was investigated. Incubation of apoPGHS-1 with 2 equiv of N-(carboxyheptyl)[3,4- 14C]maleimide led to the incorporation of radioactivity in the protein, but no adduct was detected by reversed-phase HPLC, suggesting that it was unstable to the chromatographic conditions. Furthermore, hematin- reconstituted PGHS-1, which was rapidly inhibited by N- (carboxyheptyl)maleimide, displayed spontaneous regeneration of about 50% of the cyclooxygenase and peroxidase activities, suggesting that the adduct responsible for the inhibition breaks down to regenerate active enzyme. ApoPGHS-1, inhibited by N-(carboxyheptyl)maleimide, did not display regeneration of enzyme activity, but addition of hematin to the inhibited apoenzyme led to spontaneous recovery of about 50% of cyclooxygenase activity. These results suggest that addition of heme leads to a conformational change in the protein which increases the susceptibility of the adduct toward hydrolytic cleavage. ApoPGHS-1, pretreated with N(carboxyheptyl)maleimide, was resistant to trypsin cleavage, suggesting that the carboxylate functionality of the maleimide binds in the cyclooxygenase channel. A model for the interaction of N-(carboxyheptyl)maleimide in the cyclooxygenase active site is proposed.