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 composed of the amino acids glutamic acid and threonine linked via a peptide bond. As a member of the dipeptide family, it serves as a valuable molecular tool in peptide chemistry, biochemical research, and proteomics. The presence of both an acidic side chain (from glutamic acid) and a hydroxyl-containing side chain (from threonine) imparts distinctive physicochemical properties, making this compound particularly relevant for studies involving peptide structure, enzyme specificity, and amino acid sequence motifs. Its defined sequence and manageable size allow for versatile integration into experimental models, supporting a range of investigations in protein science and beyond.
Peptide Synthesis Research: Glu-Thr is frequently utilized as a building block in solid-phase peptide synthesis and combinatorial chemistry. Its defined dipeptide structure enables researchers to explore sequence-dependent effects in synthetic peptide libraries, facilitating the design and optimization of novel peptides with tailored biological or physicochemical properties. The compound's compatibility with standard peptide coupling strategies allows for efficient incorporation into longer peptide chains, aiding in the development of complex peptide-based constructs for various research applications.
Enzyme Substrate Studies: Owing to its specific sequence, Glu-Thr serves as a substrate or sequence motif for investigating the specificity and catalytic mechanisms of proteases, peptidases, and other peptide-modifying enzymes. By incorporating this dipeptide into model substrates, researchers can probe enzyme-substrate interactions, map cleavage sites, and assess the influence of adjacent residues on enzymatic activity. Such studies are essential for elucidating the biochemical pathways involving peptide processing and for informing the design of selective enzyme inhibitors or activity assays.
Protein Structure and Folding Analysis: The unique side chain chemistry of Glu-Thr offers opportunities for examining the influence of local sequence context on protein secondary structure and folding dynamics. Researchers employ this dipeptide in model systems to study hydrogen bonding, electrostatic interactions, and conformational preferences within peptides and proteins. Insights gained from these studies contribute to a deeper understanding of sequence-structure relationships and inform computational modeling efforts in structural biology.
Analytical Method Development: Glu-Thr is employed as a reference standard or calibration compound in chromatographic and mass spectrometric analyses of peptides. Its well-defined structure and predictable fragmentation patterns make it suitable for method validation, instrument calibration, and quantitative analysis in peptide mapping workflows. The availability of such dipeptides enhances the accuracy and reproducibility of analytical protocols in proteomics, quality control, and peptide characterization.
Cellular Uptake and Transport Studies: As a small peptide, Glu-Thr is also used to investigate the mechanisms of peptide transport across biological membranes. Studies utilizing this compound help elucidate the substrate specificity and kinetics of peptide transporters, which play critical roles in nutrient absorption, cellular signaling, and drug delivery. By tracking the uptake and distribution of dipeptides like Glu-Thr, researchers can gain valuable insights into transporter-mediated processes and inform the design of peptide-based delivery systems.
1. High fat diet and GLP-1 drugs induce pancreatic injury in mice
5. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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