L-Ornithyl-L-ornithine consists of two ornithine residues joined to form a functional dipeptide strongly associated with polyamine biosynthetic studies. The dual amino side chains enhance reactivity and provide high versatility for conjugation chemistry. Structural flexibility facilitates transport and metabolic pathway modeling. Use spans protein modification research, synthetic derivatization, and enzymatic mechanism exploration.
CAT No: R2425
CAS No:60259-82-7
Synonyms/Alias:L-Ornithyl-L-ornithine;60259-82-7;L-Ornithine, N2-L-ornithyl-;(2S)-5-amino-2-[[(2S)-2,5-diaminopentanoyl]amino]pentanoic Acid;H-ORN-ORN-OH;ornithyl-ornithine;Orn-Orn;CHEMBL208960;SCHEMBL9561353;DTXSID101314598;(S)-5-Amino-2-((S)-2,5-diaminopentanamido)pentanoic acid;(S)-5-Amino-2-((S)-2,5-diaminopentanamido)pentanoicacid;
L-Ornithyl-L-ornithine is a synthetic dipeptide composed of two ornithine molecules linked via a peptide bond, offering unique biochemical properties that make it a valuable tool in various research and industrial applications. As a non-proteinogenic peptide, it is not directly incorporated into proteins but is instead leveraged for its role in nitrogen metabolism and its ability to mimic or modulate biological processes involving ornithine. The compound is characterized by its stability, solubility in aqueous environments, and compatibility with a range of experimental conditions, making it a versatile reagent for in vitro studies. Its structural features allow it to act as a model substrate or inhibitor in enzymatic assays, particularly those involving peptidases and enzymes related to the urea cycle. Researchers appreciate its utility in probing metabolic pathways, exploring peptide transport mechanisms, and developing novel biomaterials.
Metabolic Pathway Research: L-Ornithyl-L-ornithine serves as a key molecular probe for elucidating the intricacies of nitrogen metabolism, particularly in studies focused on the urea cycle and related biochemical pathways. By introducing this dipeptide into cell cultures or enzymatic systems, researchers can investigate the roles of ornithine transporters, peptidases, and other enzymes that interact with ornithine derivatives. Its presence enables the dissection of metabolic fluxes, the identification of regulatory checkpoints, and the development of mechanistic models that advance our understanding of amino acid catabolism and biosynthesis. The compound's unique structure allows for the selective tracking of metabolic intermediates, providing insights that are otherwise challenging to obtain with single amino acids.
Enzyme Substrate and Inhibitor Studies: In the realm of enzymology, L-Ornithyl-L-ornithine is frequently employed as a substrate or competitive inhibitor in assays designed to characterize the specificity and kinetics of peptidases, amidases, and other proteolytic enzymes. Its dipeptide structure enables it to mimic natural substrates, facilitating the analysis of enzyme active sites and catalytic mechanisms. Furthermore, it can be used to screen for potential inhibitors or modulators of enzymes involved in ornithine metabolism, supporting the discovery of new biochemical tools and therapeutic leads. The compound's defined peptide bond and ornithine side chains make it particularly useful for structure-activity relationship studies and the optimization of enzyme assays.
Peptide Transport Mechanism Investigation: Researchers utilize L-Ornithyl-L-ornithine to probe the activity and selectivity of peptide transporters in cellular and membrane systems. By tracking the uptake, localization, and intracellular processing of this dipeptide, scientists can delineate the substrate preferences of various transporter families, such as the proton-coupled oligopeptide transporters (POTs). Such studies are critical for understanding nutrient absorption, drug delivery, and the physiological roles of peptide transporters in health and disease. The compound's resistance to rapid degradation further enhances its value in long-term transport experiments, allowing for precise kinetic and mechanistic analyses.
Biomaterials and Peptide Engineering: The unique chemical properties of L-Ornithyl-L-ornithine make it an attractive building block for the design and synthesis of novel biomaterials and engineered peptides. Its incorporation into peptide chains can confer enhanced stability, altered charge characteristics, or specific binding affinities, expanding the functional repertoire of synthetic peptides. Researchers exploit these features to develop hydrogels, scaffolds, or functionalized surfaces for applications in tissue engineering, drug delivery, and biosensing. The dipeptide's compatibility with standard peptide synthesis protocols ensures its seamless integration into complex molecular architectures.
Analytical Method Development: Analytical chemists employ L-Ornithyl-L-ornithine as a standard or reference compound in the development and validation of chromatographic, spectroscopic, and mass spectrometric methods. Its defined molecular structure and known physicochemical properties make it ideal for calibrating instruments, optimizing separation conditions, and assessing method sensitivity and selectivity. The compound is also used in quality control procedures for peptide synthesis and purification, ensuring the accuracy and reproducibility of analytical workflows. Its application in method development supports the advancement of peptide analytics and facilitates high-precision research across multiple scientific disciplines.
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