Gly-Arg combines the flexibility of glycine with the strong basicity of arginine, enabling investigation of early folding and charge-driven interactions. The dipeptide serves as a useful probe in enzymatic recognition studies. Researchers evaluate its hydrogen-bond patterns and solution behavior. Applications span peptide synthesis development, binding analysis, and conformational modeling.
CAT No: R2630
CAS No:18635-55-7
Synonyms/Alias:Glycyl-L-arginine;H-Gly-Arg-OH;18635-55-7;L-Arginine, glycyl-;glycylarginine;Glycyl-Arginine;P56Q695EWK;Gly-Arg;Gly-L-Arg;NSC-334212;CHEBI:73860;UNII-P56Q695EWK;CHEMBL96806;(2S)-2-((2-Aminoacetyl)amino)-5-(diaminomethylideneamino)pentanoic acid;(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoic acid;(S)-2-(2-Aminoacetamido)-5-guanidinopentanoic acid;GR dipeptide;G-R Dipeptide;L-Glycyl-L-Arginine;Gly-L-Arg-OH;Glycine Arginine dipeptide;Glycine-Arginine dipeptide;2-((2-Amino-1-hydroxyethylidene)amino)-5-carbamimidamidopentanoate;2-[(2-Amino-1-hydroxyethylidene)amino]-5-carbamimidamidopentanoate;Glycinyl-L-arginine;Glycyl-L-arginine;;H-Gly-Arg;MFCD00190918;SCHEMBL187696;JLXVRFDTDUGQEE-YFKPBYRVSA-N;DTXSID801316438;HY-P4596;BDBM50407457;DA-53979;FG108046;CS-0655369;Q27144186;(2S)-2-(2-AMINOACETAMIDO)-5-CARBAMIMIDAMIDOPENTANOIC ACID;
Gly-Arg, also known as Glycyl-Arginine, is a synthetic dipeptide composed of glycine and arginine residues linked via a peptide bond. As a member of the peptide compound category, it exhibits unique biochemical properties derived from the combination of its constituent amino acids. Glycine, the simplest amino acid, contributes flexibility and minimal steric hindrance, while arginine imparts a positively charged guanidinium group, enabling diverse interactions with biomolecules. The resulting dipeptide is of particular interest in biochemical research due to its defined structure, charge characteristics, and potential for modulating cellular processes. Glycyl-Arginine serves as a valuable molecular tool for investigating peptide function, structure-activity relationships, and transport mechanisms in various experimental systems.
Peptide transport studies: Glycyl-Arginine is frequently employed as a model substrate in the study of peptide transporters, particularly those of the SLC15 family such as PEPT1 and PEPT2. Its dipeptide structure and charge distribution make it a suitable probe for elucidating the substrate specificity, kinetic parameters, and transport mechanisms of these integral membrane proteins. By monitoring the uptake and translocation of Gly-Arg across cellular membranes, researchers gain insights into the physiological and pharmacological roles of peptide transporters in nutrient absorption and drug delivery.
Enzymatic activity assays: As a defined dipeptide, Glycyl-Arginine is utilized in enzymatic assays to evaluate the specificity and catalytic efficiency of peptidases and proteases. Its sequence enables selective cleavage by enzymes with affinity for basic residues at the C-terminus, allowing for precise assessment of enzyme kinetics and substrate recognition. This application is particularly relevant in the characterization of dipeptidyl peptidases, aminopeptidases, and other proteolytic enzymes involved in peptide metabolism.
Peptide synthesis validation: Glycyl-Arginine serves as a standard reference compound in synthetic peptide chemistry. Its well-characterized structure and straightforward synthesis make it ideal for calibrating analytical methods such as high-performance liquid chromatography (HPLC) and mass spectrometry. By comparing retention times and fragmentation patterns, chemists can confirm the successful synthesis and purity of more complex peptides, thereby ensuring quality control in peptide manufacturing processes.
Cell signaling research: The presence of arginine in the dipeptide sequence allows Glycyl-Arginine to participate in studies of cell signaling pathways involving basic amino acid motifs. Researchers utilize this dipeptide to probe interactions with cellular receptors, transporters, or enzymes that recognize arginine-containing sequences. Such investigations contribute to a deeper understanding of the roles played by short peptides in modulating intracellular communication, signal transduction, and protein-protein interactions.
Nutritional and metabolic studies: Glycyl-Arginine is also applied in investigations of amino acid and peptide metabolism. Its defined composition permits the tracking of metabolic fates and the study of enzymatic pathways responsible for dipeptide hydrolysis and assimilation. By incorporating Gly-Arg into experimental systems, scientists can dissect the contributions of dipeptides to nitrogen balance, cellular energetics, and the regulation of metabolic fluxes in both prokaryotic and eukaryotic models.
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