Glu-Asp-Arg is a tripeptide featuring acidic residues balanced by a basic arginine, creating strong electrostatic character. The sequence supports research on charge-driven folding, salt-bridge formation, and substrate recognition. Researchers employ it in enzyme mapping and structural modeling. Its compact size enables precise mechanistic study.
CAT No: R2230
CAS No:175175-23-2
Synonyms/Alias:pinealon;Glu-Asp-Arg;H-Glu-Asp-Arg-OH;L-Glu-L-Asp-L-Arg;E-D-R;175175-23-2;CHEBI:156374;L-Glutamyl-L-aspartyl-L-arginine;L-alpha-glutamyl-L-alpha-aspartyl-L-arginine;glutamylaspartylarginine;glutamyl-aspartyl-arginine;SCHEMBL3839057;HY-P4052;AT42450;DA-56878;CS-0635571;(4S)-4-amino-5-[[(2S)-3-carboxy-1-[[(1S)-1-carboxy-4-(diaminomethylideneamino)butyl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoic acid;
Glu-Asp-Arg is a synthetic tripeptide composed of glutamic acid, aspartic acid, and arginine residues, arranged in a specific linear sequence. As a member of the peptide compound category, it exhibits unique physicochemical properties and biological relevance due to the distinctive side chains of its constituent amino acids. The negatively charged glutamic acid and aspartic acid residues, combined with the positively charged arginine, confer a net charge distribution that can influence molecular interactions, binding affinities, and conformational dynamics. Researchers utilize such tripeptides to probe fundamental aspects of protein structure, peptide signaling, and cellular recognition mechanisms, making Glu-Asp-Arg a valuable tool in both basic and applied biochemical studies.
Peptide structure-function analysis: Tripeptides like Glu-Asp-Arg are frequently employed as model systems for elucidating the relationship between amino acid sequence and functional properties. The specific arrangement of acidic and basic side chains in this molecule enables detailed investigations into charge-mediated folding, hydrogen bonding, and electrostatic interactions. By incorporating Glu-Asp-Arg into structural studies, scientists can gain insights into the principles governing peptide conformation, stability, and the formation of secondary structures, which are essential for understanding larger protein assemblies.
Enzyme substrate specificity studies: The defined sequence of Glu-Asp-Arg serves as a valuable substrate or inhibitor in enzymology research, particularly for enzymes that recognize or cleave specific peptide bonds. Its sequence can be used to assess the substrate preferences of proteases, peptidases, or protein-modifying enzymes, facilitating the mapping of active sites and elucidating catalytic mechanisms. Such studies are critical for characterizing enzyme selectivity, developing activity assays, and designing targeted inhibitors for biochemical pathways.
Cell signaling and receptor interaction research: The presence of both negatively and positively charged residues in Glu-Asp-Arg allows it to mimic certain motifs found in biologically active peptides involved in cell signaling. Researchers use this tripeptide to investigate peptide-receptor interactions, ligand binding affinities, and downstream cellular responses. By studying how Glu-Asp-Arg interacts with cell surface receptors or transporters, scientists can dissect the molecular determinants of signal transduction and cellular communication.
Peptide synthesis and method development: Glu-Asp-Arg is often utilized as a reference sequence or building block in the development and optimization of solid-phase peptide synthesis protocols. Its incorporation tests the efficiency of coupling reactions, deprotection strategies, and purification methods, especially given the challenges posed by its charged side chains. The tripeptide thus serves as a practical benchmark for refining synthetic techniques and ensuring the reliability of peptide production workflows.
Analytical method calibration: Due to its well-defined structure and predictable chromatographic behavior, Glu-Asp-Arg is used as a standard in analytical chemistry for calibrating peptide separation and detection systems. It assists in the validation of high-performance liquid chromatography (HPLC), mass spectrometry, and electrophoretic techniques, enabling accurate quantification and identification of peptides in complex mixtures. Utilizing this tripeptide as a calibration reference enhances the precision and reproducibility of analytical assays in peptide research and quality control settings.
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