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 dipeptide composed of the amino acids valine and arginine linked by a peptide bond. This compound is widely recognized in biochemical research for its unique physicochemical characteristics, including its stability and solubility in aqueous environments. Val-Arg exhibits a balanced profile of hydrophobic and basic properties, making it an attractive candidate for studies involving peptide transport, enzymatic activity, and molecular recognition. Researchers value its defined structure and the ability to serve as a substrate, model compound, or functional component in various experimental systems. The presence of both a branched-chain amino acid and a guanidinium-containing residue imparts versatility to Val-Arg, supporting its use in diverse scientific investigations ranging from enzymology to peptide-based delivery systems.
Peptide Transport Studies: Val-Arg is frequently employed as a model dipeptide in the investigation of peptide transport mechanisms across biological membranes. Its dual amino acid composition allows researchers to probe the specificity and efficiency of peptide transporters, such as PEPT1 and PEPT2, in both in vitro and in vivo systems. By utilizing Val-Arg, scientists can evaluate transporter affinity, substrate competition, and uptake kinetics, thereby advancing the understanding of nutrient absorption and drug delivery pathways mediated by oligopeptide carriers.
Enzyme Substrate Characterization: As a well-defined dipeptide, Valyl-Arginine serves as a valuable substrate for the study of proteolytic enzymes, including dipeptidyl peptidases and aminopeptidases. Its structure enables precise mapping of enzyme cleavage preferences, catalytic efficiency, and inhibitor screening. Researchers often use Val-Arg in kinetic assays to quantify enzyme activity, elucidate substrate specificity, and explore the mechanistic details of peptide bond hydrolysis. These insights are critical for the development of enzyme modulators and the characterization of metabolic pathways involving peptide processing.
Peptide Drug Design: In the context of pharmaceutical research, Val-Arg is utilized as a building block for the synthesis of peptide-based drug candidates and prodrugs. Its combination of hydrophobic and basic residues facilitates membrane interaction and enhances bioavailability, making it a strategic component in the design of therapeutic peptides with improved pharmacokinetic profiles. Scientists leverage the properties of Val-Arg to optimize peptide stability, target specificity, and resistance to enzymatic degradation, supporting the development of innovative drug delivery systems and bioactive compounds.
Nutritional Biochemistry: Valyl-Arginine finds application in nutritional studies focused on amino acid metabolism, absorption, and utilization. As a representative dipeptide, it is used to assess the efficiency of peptide digestion, transport, and assimilation in various biological models. Its inclusion in experimental diets or perfusion studies enables researchers to monitor metabolic flux, nitrogen balance, and the role of dipeptides in supporting growth and tissue repair. Insights gained from studies involving Val-Arg contribute to the formulation of advanced nutritional supplements and functional foods.
Analytical Method Development: Analytical chemists utilize Val-Arg as a standard or reference compound in the development and validation of chromatographic and spectrometric methods for peptide analysis. Its defined structure and predictable retention behavior make it suitable for method calibration, system suitability testing, and quality control procedures. By incorporating Val-Arg into analytical workflows, laboratories can ensure accurate quantification, reproducibility, and sensitivity when analyzing complex peptide mixtures or biological samples. This application underpins the reliability of peptide research and supports advancements in bioanalytical science.
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