L-Ornithine Dimer joins two ornithine residues to create a highly basic construct suitable for studying polyamine-like interactions. The dual amino groups enhance reactivity and electrostatic binding. Researchers evaluate its conformational preferences and solubility. Uses include metabolic modeling, synthetic modification, and protein-peptide interaction studies.
CAT No: R2517
CAS No:195868-13-4
Synonyms/Alias:L-Ornithine Dimer;195868-13-4;(2S)-2-amino-5-[[(2S)-2,5-diaminopentanoyl]amino]pentanoic acid;
L-Ornithine Dimer is a unique carbohydrate compound composed of two ornithine molecules joined together, offering distinctive physicochemical properties that set it apart from its monomeric counterpart. This dimeric structure enhances its solubility and stability, making it an attractive candidate for various research and industrial applications. With its ability to participate in biochemical pathways involving nitrogen metabolism and polyamine synthesis, L-Ornithine Dimer serves as a versatile tool for scientists seeking to explore and manipulate complex metabolic networks. Its compatibility with aqueous environments and ease of incorporation into experimental systems further broaden its potential uses across multiple scientific disciplines.
Metabolic Pathway Elucidation: In metabolic research, L-Ornithine Dimer is frequently employed to investigate the intricacies of the urea cycle and related nitrogen-handling processes. Researchers utilize this compound to trace the transformation of ornithine derivatives within cellular systems, enabling the mapping of enzymatic activities and the identification of regulatory checkpoints. By incorporating isotopically labeled forms of the dimer, scientists can precisely track the fate of nitrogen atoms and unravel the dynamic fluxes within amino acid metabolism, thus gaining deeper insights into fundamental physiological processes.
Enzyme Substrate Studies: The dimeric form of ornithine serves as a valuable substrate analog in enzymology studies. Its distinct structure allows researchers to probe the specificity and catalytic mechanisms of enzymes involved in ornithine metabolism, such as ornithine decarboxylase and transaminases. By comparing the enzymatic processing of the dimer versus the monomer, investigators can discern subtle differences in binding affinities, reaction rates, and product formation, ultimately contributing to a more comprehensive understanding of enzyme-substrate interactions and potential points of metabolic regulation.
Biochemical Assay Development: L-Ornithine Dimer is increasingly utilized in the development and optimization of biochemical assays designed to quantify ornithine-related metabolites or enzyme activities. Its enhanced stability and solubility make it an ideal standard or calibration compound in high-throughput screening platforms. Additionally, the dimer can serve as a competitive inhibitor or activator in assay systems, allowing researchers to fine-tune assay sensitivity and specificity for diverse analytical applications, including biomarker discovery and metabolic profiling.
Nutritional and Functional Food Research: In the field of nutrition science, ornithine dimers are explored for their potential to modulate amino acid availability and influence metabolic health. Researchers incorporate it into model food systems or cell culture studies to assess its effects on nutrient absorption, nitrogen balance, and protein synthesis. These investigations help elucidate the role of dimeric amino acids in dietary formulations and may inform the design of functional foods aimed at supporting metabolic wellness or athletic performance.
Polyamine Biosynthesis Investigations: The unique structural features of L-Ornithine Dimer make it a valuable probe in studies of polyamine biosynthesis, a pathway critical for cell proliferation and differentiation. Scientists employ the dimer to examine its impact on the regulation of key enzymes such as ornithine decarboxylase and to investigate the downstream production of polyamines like putrescine and spermidine. By manipulating dimer concentrations in experimental systems, researchers can dissect feedback mechanisms and uncover novel regulatory nodes within the polyamine pathway, advancing our understanding of cellular growth control and metabolic adaptation.
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