Leu-Gln balances hydrophobicity with polar amide functionality, making it a versatile dipeptide for folding and hydrogen-bond investigations. Researchers explore its role in helix and coil formation. Solvent interactions help clarify side-chain contributions to stability. Applications include peptide-assembly modeling, enzymatic recognition, and motif analysis.
CAT No: R2661
CAS No:38062-70-3
Synonyms/Alias:leucyl-glutamine;L-LEUCYL-L-GLUTAMINE;Leu-Gln;(2S)-5-amino-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-5-oxopentanoic acid;38062-69-0;38062-70-3;H-Leu-Gln-OH;L-Glutamine, L-leucyl-;SCHEMBL4221705;CHEBI:157865;JYOAXOMPIXKMKK-YUMQZZPRSA-N;DTXSID201315363;AKOS010407396;(S)-5-Amino-2-((S)-2-amino-4-methylpentanamido)-5-oxopentanoic acid;
Leu-Gln, also known as L-Leucyl-L-Glutamine or Leucine-Glutamine dipeptide, is a synthetic dipeptide composed of the essential amino acid leucine and the conditionally essential amino acid glutamine. This compound is frequently utilized in scientific research due to its unique ability to combine the metabolic and signaling properties of both constituent amino acids. Leu-Gln exhibits enhanced solubility and stability compared to free glutamine, making it a valuable additive in various experimental settings. Researchers appreciate its capacity to serve as a stable glutamine source, particularly in environments where glutamine degradation is a concern. The dipeptide's structure also facilitates efficient cellular uptake, potentially influencing cellular metabolism and signaling pathways relevant to amino acid transport and utilization.
Cell Culture Supplementation: In cell biology and biotechnological research, Leu-Gln is widely employed as a robust alternative to free glutamine in cell culture media. Its stability under standard incubation conditions prevents rapid degradation, thereby ensuring a consistent supply of glutamine to support cell growth, viability, and protein synthesis. This property is particularly advantageous during long-term cultures or high-density cell cultivation, where maintaining optimal nutrient concentrations is critical for reproducible experimental outcomes. The dipeptide form also minimizes the accumulation of toxic byproducts, such as ammonia, which can result from glutamine breakdown in culture systems.
Protein and Peptide Metabolism Studies: Leu-Gln serves as a valuable tool for investigating the metabolic fate and transport mechanisms of dipeptides in mammalian cells. Researchers utilize it to dissect the pathways involved in dipeptide uptake, hydrolysis, and intracellular utilization, thereby contributing to a deeper understanding of amino acid absorption and metabolism. Such studies are especially relevant in the context of peptide transporter function and the regulation of nutrient sensing pathways. By using Leu-Gln, scientists can differentiate between the effects mediated by free amino acids and those uniquely attributed to dipeptide forms.
Nutritional Biochemistry Research: The dipeptide Leu-Gln is often incorporated into experimental models exploring the bioavailability and metabolic effects of peptide-bound amino acids. Its dual composition allows researchers to simultaneously examine the roles of leucine and glutamine in protein synthesis, energy metabolism, and cellular signaling. This approach is particularly useful in studies focused on muscle protein turnover, energy homeostasis, and the interplay between amino acid supplementation and metabolic adaptation. The use of Leu-Gln in such research provides insights into the physiological relevance of dipeptide supplementation compared to free amino acids.
Transporter Mechanism Elucidation: Leu-Gln is instrumental in the study of peptide transporters, such as PEPT1 and PEPT2, which mediate the uptake of di- and tripeptides across cell membranes. By tracking the cellular uptake and intracellular fate of Leu-Gln, researchers can characterize the specificity, kinetics, and regulatory mechanisms of these transporters. This information is critical for understanding nutrient absorption in the intestine and kidney, as well as for developing targeted delivery systems for peptide-based therapeutics and nutrients.
Bioprocess Optimization: In the field of industrial biotechnology, Leu-Gln is utilized to optimize fermentation processes and enhance recombinant protein production. Its superior stability reduces the risk of nutrient depletion and toxic metabolite accumulation, supporting higher cell densities and improved product yields. By providing a reliable source of glutamine and leucine, the dipeptide enables consistent bioprocess performance, facilitating the scale-up of cell-based manufacturing systems. Researchers leverage these properties to fine-tune media formulations and process parameters for maximum productivity and reproducibility. Overall, Leu-Gln's versatility and unique biochemical properties make it an indispensable tool in diverse scientific and industrial research applications, from basic metabolic studies to advanced bioprocess engineering.
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