33544-40-0

Basic information

• Product Name: 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER
• Synonyms: 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER
• CAS NO: 33544-40-0
• Molecular Formula: C₉H₁₈N₂O₂
• Molecular Weight: 186.25
• Mol File: 33544-40-0.mol
• Article Data: 10

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER(33544-40-0)
• EPA Substance Registry System: 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER(33544-40-0)

Safety Data

• Hazardous Substances Data: 33544-40-0(Hazardous Substances Data)

Usage

Description

4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER is a chemical compound that is commonly used in pharmaceutical research and development. It is a derivative of piperazine, a heterocyclic compound with various applications in the pharmaceutical industry. 4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER has attracted interest due to its potential as a precursor in the synthesis of novel drugs and its ability to modify the activity of certain biological targets. It is also known for its role in the preparation of various pharmaceutical intermediates, making it a valuable chemical in the synthesis of new drug candidates.
Used in Pharmaceutical Research and Development:
4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER is used as a precursor in the synthesis of novel drugs for its potential to modify the activity of certain biological targets.
Used in Drug Synthesis:
4-METHYL-1-PIPERAZINEPROPANOIC ACID METHYL ESTER is used as a valuable chemical in the preparation of various pharmaceutical intermediates, contributing to the development of new drug candidates.

Upstream product

• 109-01-3 1-methyl-piperazine 
• 292638-85-8 acrylic acid methyl ester 

Downstream Products

• 5317-33-9 3-(4-methyl-1-piperazinyl)-1-propanol 
• 24636-93-9 3-(4-methylpiperazin-1-yl)propionic acid hydrazide 

Relevant articles and documents

Lipase immobilization on hyroxypropyl methyl cellulose support and its applications for chemo-selective synthesis of β-amino ester compounds

The present study carried out the synthesis of β-amino ester compounds using lipase immobilized on hyroxypropyl methyl cellulose (HMC) support. Initially various lipases (biocatalysts) from different origin were immobilized and subsequently screened to obtain the robust biocatalyst. The lipase Pseudomonas fluorescence (PFL) immobilized on HMC was displayed highest lipase activity, protein content and retention of activity. The physical and biochemical characterization verified immobilization of lipase PFL on the HMC support. This immobilized biocatalyst HMC:PFL (3.5:1) was successfully applied for the practical biocatalytic applications to synthesize variety of β-amino esters. Various eight reaction parameters were optimized in details to achieve the maximum yield and chemo-selectively. The developed biocatalytic protocol was successfully applied to synthesize different industrially important β-amino esters compounds (21 substrates) with an excellent yield (>90%) and remarkable chemo selectivity (>94%). Interestingly, the immobilized HMC:PFL lipase showed 2.1–2.5 folds higher bio-catalytic activity and five times recyclability as compared to the free PFL. The plausible mechanism for lipase catalyzed synthesis of β-amino ester compounds was also proposed.

Efficient and reusable ionic liquid stabilized magnetic cobalt nanoparticles as catalysts for aza- and thia-Michael reactions

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Lipase-catalyzed aza-michael reaction on acrylate derivatives

A methodology has been developed for an efficient and selective lipase-catalyzed aza-Michael reaction of various amines (primary and secondary) with a series of acrylates and alkylacrylates. Reaction parameters were tuned, and under the optimal conditions it was found that Pseudomonas stutzeri lipase and Chromobacterium viscosum lipase showed the highest selectivity for the aza-Michael addition to substituted alkyl acrylates. For the first time also, some CLEAs were examined that showed a comparable or higher selectivity and yield than the free enzymes and other formulations.