Arg-Asp is a dipeptide forming strong electrostatic polarity due to its charged termini. Researchers use it to study salt-bridge formation, protonation behavior, and local conformational changes. The motif aids investigation into charge distribution effects on peptide stability. Its simplicity supports targeted mechanistic assays.
CAT No: R2415
CAS No:15706-88-4
Synonyms/Alias:15706-88-4;Arg-Asp;H-ARG-ASP-OH;arginylaspartic acid;L-arginyl-L-aspartic acid;Arginylaspartate;RD dipeptide;R-D Dipeptide;L-Aspartic acid, L-arginyl-;Arginyl-Aspartic acid;L-Arginyl-L-Aspartate;Arginine Aspartate dipeptide;Arginine-Aspartate dipeptide;CHEBI:73812;H-Arg-Asp-OH acoh;(2S)-2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]butanedioic acid;Arg-Asp-OH;Arginyl-Aspartate;(S)-2-((S)-2-Amino-5-guanidinopentanamido)succinic acid;L-Arg-L-Asp;DTXSID10431265;N-L-Arginyl-L-aspartic acid;(2S)-2-(((2S)-2-amino-5-(diaminomethylideneamino)pentanoyl)amino)butanedioic acid;(2S)-2-(((2S)-2-azaniumyl-5-(diaminomethylideneazaniumyl)pentanoyl)amino)butanedioate;(2S)-2-[[(2S)-2-azaniumyl-5-(diaminomethylideneazaniumyl)pentanoyl]amino]butanedioate;N-Arginylaspartate;MFCD00055818;N-Arginylaspartic acid;N-L-Arginyl-L-aspartate;SCHEMBL1736042;Arginine aspartic acid dipeptide;Arginine-aspartic acid dipeptide;DTXCID20382097;HY-P4252;RD;AKOS030240418;AT16736;DA-64025;CS-0653336;Q27144128;(S)-2-((S)-2-Amino-5-guanidinopentanamido)succinicacid;(2S)-2-[(2S)-2-amino-5-[(diaminomethylidene)amino]pentanamido]butanedioic acid;
Arg-Asp, also known as Arginyl-Aspartic Acid, is a synthetic dipeptide composed of the amino acids arginine and aspartic acid linked by a peptide bond. As a member of the peptide compound category, Arg-Asp exhibits unique physicochemical properties that make it valuable for various biochemical and molecular research applications. The presence of both a basic (arginine) and an acidic (aspartic acid) residue within its structure imparts distinctive charge characteristics, influencing its interactions with proteins, enzymes, and cellular components. Researchers frequently utilize dipeptides like Arg-Asp to probe peptide structure-function relationships, investigate cellular uptake mechanisms, and explore the role of short peptides in biological signaling and molecular recognition processes.
Peptide synthesis research: Arg-Asp serves as a model dipeptide in the study and optimization of peptide synthesis protocols. Its sequence, containing both a positively charged guanidinium group from arginine and a negatively charged carboxylate from aspartic acid, provides a representative system for evaluating coupling efficiency, protecting group strategies, and purification methods in solid-phase and solution-phase peptide synthesis workflows. By incorporating Arg-Asp into synthetic schemes, researchers can assess the impact of sequence composition on yield, purity, and solubility, thereby refining methodologies for larger or more complex peptide targets.
Protein-peptide interaction studies: The unique charge distribution and side-chain functionalities of Arg-Asp make it a useful probe for investigating protein-peptide interactions, particularly those mediated by electrostatic or hydrogen bonding forces. It is often employed in binding assays, structural biology experiments, and computational modeling to elucidate the molecular determinants of recognition between short peptides and protein domains such as SH3, PDZ, or integrin-binding motifs. Such studies contribute to a deeper understanding of signaling pathways, regulatory mechanisms, and the design of peptide-based modulators.
Enzyme substrate specificity assays: Dipeptides like Arg-Asp are frequently utilized as substrates or competitive inhibitors in enzymatic assays aimed at characterizing the specificity and catalytic mechanisms of proteases, peptidases, and other hydrolytic enzymes. By monitoring the cleavage or modification of Arg-Asp, researchers can delineate the substrate preferences and kinetic properties of enzymes involved in peptide metabolism, which is critical for drug discovery, inhibitor design, and the elucidation of metabolic pathways.
Cellular uptake and transport research: The transport of small peptides across biological membranes is a topic of significant interest in pharmacology and cell biology. Arg-Asp is employed as a model compound to study the activity of peptide transporters, such as those in the SLC15 family, under various physiological and experimental conditions. By tracing its uptake in cultured cells or membrane vesicle systems, investigators gain insights into the molecular determinants governing peptide absorption, distribution, and bioavailability, which can inform the design of peptide-based delivery systems.
Analytical method development: The well-defined structure and charge properties of Arg-Asp make it a suitable standard or reference compound in the development and validation of analytical techniques, including high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its use as a calibration standard or system suitability test compound aids in the assessment of method sensitivity, selectivity, and reproducibility, supporting robust analytical workflows in peptide research and quality control laboratories.
1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
2. C-Peptide replacement therapy and sensory nerve function in type 1 diabetic neuropathy
3. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
4. High fat diet and GLP-1 drugs induce pancreatic injury in mice
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