23684-48-2

Usage

Uses

Used in Neuropharmacology:
H-GLU-GLU-GLU-OH is used as a potential drug candidate in neuropharmacology for its role in neurotransmission and involvement in various neurological functions. Its ability to modulate glutamate receptors may contribute to the treatment of neurological disorders.
Used in Drug Development:
H-GLU-GLU-GLU-OH is utilized as a building block in the development of novel drugs targeting the central nervous system. Its unique properties and interactions with neurotransmitter systems offer opportunities for creating therapeutic agents with specific mechanisms of action.
Used in Research and Biotechnology:
H-GLU-GLU-GLU-OH is employed as a research tool in biotechnology for studying protein-protein interactions and the development of targeted drug delivery systems. Its chemical structure and properties allow for the exploration of its potential in modulating biological processes and improving drug targeting and delivery.
Used in Drug Delivery Systems:
H-GLU-GLU-GLU-OH is used as a component in the design of drug delivery systems, particularly for central nervous system-targeted therapies. Its ability to interact with neurotransmitter systems and its potential to enhance drug penetration into the brain make it a valuable asset in the development of advanced drug delivery technologies.

Upstream product

• 56-86-0 L-glutamic acid 
• 74-79-3 L-arginine 
• 79-14-1 glycolic Acid 

Relevant academic research and scientific papers

Ester-mediated peptide formation promoted by deep eutectic solvents: a facile pathway to proto-peptides

The ester-amide exchange reaction enables spontaneous formation of prebiotic proto-peptides under mild conditions. However, this reaction also leads to oligomers with a vast sequence diversity of ester and amide linkages. Here, we demonstrate using deep eutectic solvents as a universal strategy to regulate the reaction pathways and promote the formation of amino acid-enriched oligomers with peptide backbones.

Modelling of prebiotic synthesis and selection of peptides under isothermal conditions and thermal cycling mode

The model peptide synthesis from mixtures of amino acids was carried out under the thermal cycling and isothermal modes. The compositions of the obtained mixtures of products and the primary amino acid sequence of the synthesized peptides were determined by Fourier transform ion cyclotron resonance mass spectrometry and tandem mass spectrometry in combination with high-performance liquid chromatography with the application of de novo sequencing of the synthesized products. The processes of abiogenous synthesis of peptides were shown to occur under relatively mild temperature conditions and give a substantially less number of peptides as compared with the possible statistical set. The evolution of the system takes place in the process of the synthesis in solid phase with the disappearance of a series of the most unstable peptides. The selection process with the formation of complementary peptides takes place in peptide synthesis under the thermal cyclic mode.

The Relationship between Taste and Primary Structure of "Delicious Peptide" (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) from Beef Soup

"Delicious peptide" was reported to be as delicious as beef soup.The peptide and its fragments were synthesized to study its taste active sites. "Delicious peptide" was found to produce a umami and a sour taste.By preparing several di- or tripeptides composed of basic or acidic amino acids, we found that the taste of "delicious peptide" was produced by an interaction between the basic and the acidic fragments in the peptide.