5649-49-0

Basic information

• Product Name: 1,4-BIS(2-CARBOXYETHYL)PIPERAZINE
• Synonyms: 1,4-BIS(2-CARBOXYETHYL)PIPERAZINE;Biscarboxyethylpiperazine;piperazine-1,4-dipropionic acid;1,4-BIS(2-CARBOXYETHYL)PIPERAZINE 97+%;1,4-Piperazinedipropanoic acid;1,4-Piperazinedipropionic acid;3-[4-(2-carboxyethyl)piperazin-1-yl]propanoic acid;3-[4-(2-carboxyethyl)piperazin-1-yl]propionic acid
• CAS NO: 5649-49-0
• Molecular Formula: C₁₀H₁₈N₂O₄
• Molecular Weight: 230.26
• EINECS: 227-088-5
• Mol File: 5649-49-0.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 458.1°Cat760mmHg
• Flash Point: 230.8°C
• Appearance: /
• Density: 1.238g/cm³
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: 1,4-BIS(2-CARBOXYETHYL)PIPERAZINE(CAS DataBase Reference)
• NIST Chemistry Reference: 1,4-BIS(2-CARBOXYETHYL)PIPERAZINE(5649-49-0)
• EPA Substance Registry System: 1,4-BIS(2-CARBOXYETHYL)PIPERAZINE(5649-49-0)

Safety Data

• Statements: 36/37/38
• Safety Statements: 26-36/37/39
• Hazardous Substances Data: 5649-49-0(Hazardous Substances Data)

Usage

General Description

1,4-Bis(2-carboxyethyl)piperazine, also known as BCEP, is a chemical compound with the molecular formula C12H23N3O4. It is a versatile compound that is often used in industrial applications as a corrosion inhibitor and as a chelating agent in water treatment processes. BCEP is also utilized in the pharmaceutical industry as a building block for the synthesis of various medicinal compounds and as a stabilizer for various drugs. Additionally, BCEP has been studied for its potential use in the development of materials for drug delivery systems and as a precursor for the production of polymers and other organic compounds. Due to its diverse range of applications, BCEP is an important and valuable chemical compound in various industries.

Upstream product

• 110-85-0 piperazine 
• 50-00-0 formaldehyd 
• 141-82-2 malonic acid 
• 590-92-1 3-Bromopropionic acid 
• 142-63-2 piperazine hexahydrate 

Relevant articles and documents

Optimization of Cyclic Plasmin Inhibitors: From Benzamidines to Benzylamines

New macrocyclic plasmin inhibitors based on our previously optimized P2-P3 core segment have been developed. In the first series, the P4 residue was modified, whereas the 4-amidinobenzylamide in P1 position was maintained. The originally used P4 benzylsulfonyl residue could be replaced by various sulfonyl- or urethane-like protecting groups. In the second series, the P1 benzamidine was modified and a strong potency and excellent selectivity was retained by incorporation of p-xylenediamine. Several analogues inhibit plasmin in the subnanomolar range, and their potency against related trypsin-like serine proteases including trypsin itself could be further reduced. Selected derivatives have been tested in a plasma fibrinolysis assay and are more effective than the reference inhibitor aprotinin. The crystal structure of one inhibitor was determined in complex with trypsin. The binding mode reveals a sterical clash of the inhibitor's linker segment with the 99-hairpin loop of trypsin, which is absent in plasmin.

Development of new cyclic plasmin inhibitors with excellent potency and selectivity

The trypsin-like serine protease plasmin is a target for the development of antifibrinolytic drugs for use in cardiac surgery with cardiopulmonary bypass or organ transplantations to reduce excessive blood loss. The optimization of our recently described substrate-analogue plasmin inhibitors, which were cyclized between their P3 and P2 side chains, provided a new series with improved efficacy and excellent selectivity. The most potent inhibitor 8 binds to plasmin with an inhibition constant of 0.2 nM, whereas Ki values >1 μM were determined for nearly all other tested trypsin-like serine proteases, with the exception of trypsin, which is also inhibited in the nanomolar range. Docking studies revealed a potential binding mode in the widely open active site of plasmin that explains the strong potency and selectivity profile of these inhibitors. The dialkylated piperazine-linker segment contributes to an excellent solubility of all analogues. Based on their overall profile the presented inhibitors are well suited for further development as injectable antifibrinolytic drugs.