Glu-Thr pairs an acidic residue with a polar side chain that enables studies of hydrogen bonding and charge distribution. Researchers evaluate its conformational preferences in aqueous systems. The dipeptide offers a platform for modeling protonation effects. Applications include peptide-folding analysis, synthesis design, and recognition studies.
CAT No: R2346
CAS No:6875-80-5
Synonyms/Alias:H-GLU-THR-OH;Glu-Thr;6875-80-5;l-glutamyl-l-threonine;(4S)-4-amino-5-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-5-oxopentanoic acid;glutamylthreonine;ET dipeptide;E-T Dipeptide;L-Glu-L-Thr;Glutamate Threonine dipeptide;Glutamate-Threonine dipeptide;L-alpha-glutamyl-L-threonine;L-I+/--Glutamyl-L-threonine;SCHEMBL4388333;CHEBI:73510;(S)-4-Amino-5-(((1S,2R)-1-carboxy-2-hydroxyPropyl)amino)-5-oxopentanoic acid;DTXSID701313162;FG108039;CS-0968597;Q27140591;(S)-4-amino-5-((1S,2R)-1-carboxy-2-hydroxypropylamino)-5-oxopentanoic acid;E-T;
Glu-Thr, also known as Glutamyl-Threonine, is a dipeptide formed by the condensation of glutamic acid and threonine via a peptide bond. Characterized by its unique combination of acidic and hydroxyl-containing amino acid residues, Glu-Thr offers considerable versatility for research and development purposes. The presence of both a carboxyl side chain from glutamic acid and a hydroxyl group from threonine imparts specific chemical reactivity, making it a valuable building block in peptide synthesis and biochemical studies. Its solubility in aqueous environments and compatibility with various analytical techniques further enhance its utility in laboratory workflows, enabling precise manipulation and integration into complex experimental systems.
Peptide Synthesis Research: Glu-Thr serves as an essential component in the assembly of custom peptides, facilitating the exploration of structure-activity relationships and the design of novel bioactive sequences. Researchers can incorporate this dipeptide into larger polypeptides to investigate the effects of specific residue placements on peptide folding, stability, and function. Its availability as a ready-to-use dipeptide simplifies the synthesis process, allowing for the rapid generation of libraries for high-throughput screening or mechanistic studies. Additionally, it can be utilized as a model substrate to optimize coupling conditions and evaluate the efficiency of peptide bond formation under various experimental parameters.
Protein Engineering: In the field of protein engineering, Glutamyl-Threonine is a useful motif for probing the influence of specific amino acid combinations within proteins. By strategically inserting this dipeptide into engineered protein sequences, scientists can study the impact on protein conformation, solubility, and intermolecular interactions. Such modifications are instrumental in the rational design of proteins with enhanced or novel functionalities, as well as in the elucidation of sequence determinants that govern protein folding pathways. The distinct chemical properties of its constituent amino acids make Glu-Thr particularly valuable in fine-tuning the physicochemical characteristics of recombinant proteins.
Enzymatic Activity Assays: Glu-Thr finds application as a substrate or reference compound in enzymatic activity assays, particularly those involving peptidases or proteases that recognize or cleave specific dipeptide bonds. By monitoring the enzymatic hydrolysis of Glu-Thr, researchers can assess the specificity and kinetics of target enzymes, screen for inhibitors, or characterize novel catalytic activities. The well-defined structure of this dipeptide enables accurate quantification and reproducibility in assay development, contributing to robust and reliable biochemical analyses.
Biochemical Pathway Elucidation: The use of Glutamyl-Threonine in metabolic and signaling pathway studies allows researchers to trace the fate of specific dipeptide motifs within cellular systems. By introducing isotopically labeled or chemically modified variants, scientists can monitor the uptake, transformation, and incorporation of Glu-Thr in metabolic networks. This approach aids in identifying key enzymes, transporters, and regulatory nodes involved in peptide metabolism, providing insights into fundamental biological processes and potential targets for intervention.
Analytical Method Development: The distinctive chromatographic and spectroscopic properties of Glu-Thr make it an ideal standard or reference compound in the development and validation of analytical methods. It can be employed in high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis protocols to calibrate instruments, optimize separation conditions, and establish detection limits for dipeptides. The consistent performance and chemical stability of Glu-Thr contribute to the generation of high-quality analytical data, supporting a wide range of research and quality control applications.
Structural Biology Studies: In structural biology, Glutamyl-Threonine plays a role in model system development for investigating peptide backbone conformations and side chain interactions. Researchers utilize this dipeptide in nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and computational modeling to analyze hydrogen bonding patterns, torsional angles, and solvation effects. The insights gained from such studies enhance the understanding of peptide and protein structure, dynamics, and function, informing the rational design of biomolecules with desired properties. By integrating Glu-Thr into diverse experimental frameworks, scientists can address complex questions in molecular biology, biochemistry, and materials science, underscoring its significance as a versatile tool in carbohydrate compound research.
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