Val-Arg pairs a hydrophobic valine with a strongly basic arginine to demonstrate contrasting side-chain behavior in small peptide systems. The dipeptide aids investigations of charge-driven binding and hydrogen-bond patterns. Its amphipathic nature supports modeling of membrane-associated interactions. Common applications include enzymatic specificity studies and synthetic method development.
CAT No: R2615
CAS No:37682-75-0
Synonyms/Alias:Val-Arg;H-Val-Arg-OH;L-valyl-L-arginine;37682-75-0;valylarginine;L-Val-L-Arg;valyl-arginine;CHEBI:73711;(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid;VR dipeptide;V-R Dipeptide;(2S)-2-(((2S)-2-amino-3-methylbutanoyl)amino)-5-(diaminomethylideneamino)pentanoic acid;MFCD00238268;L-Valinyl-L-arginine;Valine Arginine dipeptide;Valine-Arginine dipeptide;SCHEMBL7098551;DTXSID101317778;HY-P4659;DA-64304;FV108254;CS-0655661;Q27144061;(S)-2-((S)-2-Amino-3-methylbutanamido)-5-guanidinopentanoic acid;V-R;
Val-Arg, also known as Valyl-Arginine, is a synthetic dipeptide composed of the amino acids valine and arginine linked via a peptide bond. As a member of the dipeptide class, it serves as a valuable tool in biochemical and peptide research due to its defined sequence and physicochemical properties. The combination of a branched-chain, hydrophobic residue (valine) and a positively charged, basic residue (arginine) imparts unique structural and functional characteristics, making this compound highly relevant for studies in protein engineering, enzymology, and peptide transport. Its defined structure allows for precise investigation of peptide interactions, stability, and cellular uptake mechanisms, supporting a range of experimental applications in the life sciences.
Peptide transport studies: Valyl-Arginine is frequently utilized as a model substrate for examining peptide transport systems, particularly those involving oligopeptide transporters in cell membranes. By tracking its uptake and metabolism, researchers can elucidate the specificity, kinetics, and regulatory mechanisms of peptide transporters in various biological systems. This application is critical for advancing the understanding of nutrient absorption, drug delivery, and the molecular basis of peptide-mediated signaling pathways.
Enzymatic substrate analysis: As a dipeptide with a specific sequence, Val-Arg serves as an ideal substrate for investigating the activity and specificity of various peptidases and proteases. Its defined structure enables researchers to study enzyme-substrate interactions, cleavage preferences, and catalytic efficiency. This information is instrumental for characterizing enzyme function, developing enzyme inhibitors, and designing assays for high-throughput screening in drug discovery or fundamental enzymology research.
Peptide structure-function relationship studies: The distinct physicochemical properties of Valyl-Arginine make it a valuable probe for exploring the relationship between peptide sequence and biological activity. Researchers employ this dipeptide to assess how variations in amino acid composition influence secondary structure, solubility, and interaction with other biomolecules. Such studies provide insights into the principles governing peptide folding and function, informing the rational design of novel bioactive peptides and peptidomimetics.
Analytical standard for method development: In analytical biochemistry, Val-Arg is often used as a reference compound or calibration standard in chromatographic and mass spectrometric assays. Its well-characterized properties facilitate the validation and optimization of analytical methods for peptide detection, quantification, and purity assessment. Employing this dipeptide as a standard enhances the reliability and reproducibility of analytical workflows in peptide research and quality control laboratories.
Peptide synthesis optimization: The synthesis and purification of Valyl-Arginine provide a practical benchmark for evaluating peptide coupling strategies, protecting group chemistry, and purification protocols. By incorporating it into synthetic workflows, researchers can optimize reaction conditions, assess the efficiency of peptide bond formation, and troubleshoot challenges associated with the assembly of more complex oligopeptides. This application is particularly valuable for laboratories engaged in custom peptide synthesis or process development for research-use peptides.
2. Cationic cell-penetrating peptides are potent furin inhibitors
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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