5649-49-0

Usage

Uses

Used in Industrial Applications:
1,4-BIS(2-CARBOXYETHYL)PIPERAZINE is used as a corrosion inhibitor to protect materials from degradation caused by chemical or electrochemical reactions in various industrial processes. Its chelating properties also make it an effective agent in water treatment processes, where it helps to remove impurities and maintain water quality.
Used in Pharmaceutical Industry as a Building Block:
1,4-BIS(2-CARBOXYETHYL)PIPERAZINE is used as a building block for the synthesis of various medicinal compounds. Its chemical structure allows for the creation of new drugs with potential therapeutic effects, contributing to the development of novel pharmaceuticals.
Used in Pharmaceutical Industry as a Stabilizer:
1,4-BIS(2-CARBOXYETHYL)PIPERAZINE is used as a stabilizer for various drugs to enhance their shelf life and maintain their efficacy. Its ability to form stable complexes with active pharmaceutical ingredients helps to prevent degradation and ensure the consistent performance of medications.
Used in Drug Delivery Systems Development:
1,4-BIS(2-CARBOXYETHYL)PIPERAZINE is studied for its potential use in the development of materials for drug delivery systems. Its properties may contribute to the design of innovative drug carriers that can improve the bioavailability, targeting, and release of therapeutic agents.
Used as a Precursor in Polymer and Organic Compounds Production:
1,4-BIS(2-CARBOXYETHYL)PIPERAZINE is used as a precursor for the production of polymers and other organic compounds. Its versatile chemical structure allows it to be incorporated into the synthesis of a wide range of materials, expanding its applications in various industries.

Upstream product

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

Relevant academic research and scientific papers

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.

CYCLIC TRIPEPTIDE MIMETICS AS PLASMIN INHIBITORS

The invention relates to peptide mimetics comprising the residues P4-P3-P2-P1, which were cyclized between the side chains of P3 and P2 amino acid and are, as inhibitors of the serine protease plasmin, suitable to be used to inhibit fibrinolysis and thus to reduce blood loss in hyperfibrinolytic conditions, for example during surgery.

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.

Steric and electronic considerations on N,N′-piperazin-dipropionic acid as ligand

Steric and electronic ligand properties of the N,N′-piperazin-dipropionic acid, PDPA, have been investigated using the MM+ force field and the AMI MO semiempirical method. The conformational analysis evidenced the large number of PDPA low energy conformers. The barriers to rotation of the side chain bonds also showed the PDPA capability to adopt easily conformations suited for the coordination at different metal centers. The gap between HOMO and LEMO energy classifies PDPA as a hard to intermediate base. Net atomic charges and 3D-electrostatic potentials show important negative zones around the piperazine N and carboxylic O donor atoms of PDPA. Its capability to act as a tetradentate ligand is evidenced by modeling different low energy conformers of Co(II) mononuclear complexes.