Arginylproline is a dipeptide containing a charged guanidinium group and a conformationally restricted proline ring. The motif supports exploration of electrostatic interactions, backbone curvature, and β-turn mimicry. Researchers use it to investigate peptide-protein interfaces and folding pathways. Its compact design aids mechanistic mapping.
CAT No: R2316
CAS No:2418-69-1
Synonyms/Alias:Arginylproline;Arg-pro;2418-69-1;L-Arginyl-L-Proline;H-Arg-Pro-OH;arginyl-proline;RP dipeptide;H-ARG-PRO-OH SULFATE SALT;R-P Dipeptide;Arginine Proline dipeptide;Arginine-Proline dipeptide;L-Proline, 1-L-arginyl-;CHEMBL48223;(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carboxylic acid;CHEBI:141419;DTXSID70178886;arginine-proline;(2S)-1-((2S)-2-Amino-5-carbamimidamidopentanoyl)pyrrolidine-2-carboxylate;(2S)-1-[(2S)-2-Amino-5-carbamimidamidopentanoyl]pyrrolidine-2-carboxylate;1-Arginylproline;Substance P1-2;1-2-Substance p;L-Arg-L-pro;1-L-Arginyl-L-proline;SCHEMBL1674799;DTXCID30101377;RP;BDBM50049715;AKOS030622984;FA108240;HY-117110;CS-0063745;(2S)-1-[(2S)-2-AMINO-5-CARBAMIMIDAMIDOPENTANOYL]PYRROLIDINE-2-CARBOXYLIC ACID;
Arginylproline is a dipeptide composed of the amino acids arginine and proline, linked via a peptide bond. As a member of the dipeptide class, it possesses unique physicochemical properties derived from its constituent residues, including the basic guanidinium group of arginine and the cyclic secondary amine of proline. This combination imparts distinctive conformational and functional characteristics, making arginylproline of interest for a range of biochemical and molecular research applications. Due to its defined sequence and structure, it serves as a valuable tool in peptide science, structure-activity relationship studies, and the investigation of peptide-mediated biological processes.
Peptide structure-function analysis: Arginylproline is frequently utilized in studies aimed at elucidating the relationship between peptide sequence and biological activity. Its incorporation into synthetic peptide libraries allows researchers to systematically probe the impact of dipeptide motifs on protein-protein interactions, receptor binding, or enzymatic recognition. The presence of both a basic and a conformationally constrained residue enables detailed examination of how side-chain chemistry and backbone rigidity affect overall peptide behavior, informing the rational design of bioactive peptides and peptidomimetics.
Protease substrate and specificity studies: The dipeptide is a useful model substrate for investigating the specificity of various proteolytic enzymes, particularly those that recognize arginine or proline residues at defined positions. By monitoring the hydrolysis of arginylproline by endopeptidases or exopeptidases, researchers can gain insights into enzyme-substrate recognition mechanisms, substrate preference, and catalytic efficiency. Such studies are fundamental for characterizing protease function, developing enzyme inhibitors, and profiling proteolytic activity in complex biological samples.
Peptide transport and metabolism research: Arginylproline serves as a probe for studying peptide uptake and metabolism in cellular systems. Its defined structure makes it suitable for experiments examining the transport of dipeptides across cellular membranes via peptide transporters such as PEPT1 and PEPT2. Investigations using this dipeptide can reveal transporter substrate specificity, uptake kinetics, and the influence of structural features on cellular absorption, thereby contributing to a deeper understanding of nutrient assimilation and peptide pharmacokinetics in model systems.
Analytical method development: The defined physicochemical properties of arginylproline, including its solubility and chromatographic behavior, make it an effective standard or reference compound for optimizing analytical techniques such as high-performance liquid chromatography (HPLC), capillary electrophoresis, and mass spectrometry. Method validation using this dipeptide supports accurate quantification, resolution, and identification of peptides in complex mixtures, which is essential for proteomics, peptide mapping, and quality control in peptide synthesis workflows.
Peptide synthesis and optimization: In the field of synthetic peptide chemistry, arginylproline is used as a building block for the assembly of longer peptides or as a model system to study coupling efficiency and side-chain protection strategies. Its inclusion in synthetic protocols provides insight into the reactivity of arginine and proline residues during solid-phase peptide synthesis, as well as the impact of sequence context on yield and purity. Such knowledge is vital for optimizing synthesis conditions and advancing the development of complex peptide-based research tools.
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