Lysyl-Isoleucine pairs a basic lysine with a hydrophobic isoleucine, modeling amphipathic folding and charge-hydrophobic interplay. Researchers evaluate its behavior in enzyme-recognition assays. The dipeptide supports early-stage structural modeling. Applications include peptide-assembly analysis, motif exploration, and folding studies.
CAT No: R2562
CAS No:20556-13-2
Synonyms/Alias:Lysyl-Isoleucine;20556-13-2;Lys-Ile;H-LYS-ILE-OH;L-Isoleucine, L-lysyl-;L-lysyl-L-isoleucine;(2S,3S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-3-methylpentanoic acid;lysylisoleucine;L-Lys-L-Ile;KI dipeptide;K-I Dipeptide;Lysine Isoleucine dipeptide;Lysine-Isoleucine dipeptide;SCHEMBL14941410;CHEBI:74559;DTXSID60426661;Q27144735;(2S,3S)-2-((S)-2,6-diaminohexanamido)-3-methylpentanoic acid;(2S,3S)-2-(((S)-2,6-Diaminohexanoyl)amino)-3-methylpentanoic acid;(2S,3S)-2-[(2S)-2,6-DIAMINOHEXANAMIDO]-3-METHYLPENTANOIC ACID;
Lysyl-Isoleucine is a synthetic dipeptide composed of the amino acids lysine and isoleucine, joined via a peptide bond. As a representative of dipeptide compounds, it serves as a valuable molecular tool in biochemical research, owing to its defined sequence and side-chain functionalities. The presence of both a basic ε-amino group from lysine and a hydrophobic branched-chain from isoleucine imparts unique physicochemical characteristics, making it relevant for investigations into peptide structure, function, and interactions. Researchers utilize such dipeptides to model peptide behavior, study proteolytic processes, and explore sequence-specific effects in various biological and analytical contexts.
Peptide metabolism research: Lysyl-Isoleucine is frequently employed in studies of proteolytic enzymes, particularly those involved in dipeptide hydrolysis and specificity. Its defined structure enables researchers to investigate the substrate preferences and catalytic mechanisms of peptidases and dipeptidyl aminopeptidases. By monitoring the enzymatic cleavage of this dipeptide, scientists can elucidate the kinetics and selectivity of proteolytic pathways, contributing to a broader understanding of peptide turnover and regulation in biological systems.
Peptide synthesis validation: As a model dipeptide, lysyl-isoleucine is valuable for optimizing and validating solid-phase or solution-phase peptide synthesis protocols. Its well-characterized sequence allows researchers to assess coupling efficiency, side-chain protection strategies, and purification processes. The compound serves as a reference standard in analytical methods such as HPLC and mass spectrometry, ensuring reproducibility and accuracy in peptide production workflows.
Protein interaction studies: The unique side chains of lysine and isoleucine within this dipeptide provide a platform for probing sequence-dependent binding events. Researchers utilize lysyl-isoleucine in assays designed to investigate protein-peptide interactions, such as those involving recognition motifs or allosteric sites. Its defined structure aids in dissecting the contribution of specific amino acid residues to binding affinity, specificity, and conformational dynamics in protein complexes.
Analytical method development: Lysyl-isoleucine serves as a useful calibrant and reference compound in the development and validation of analytical techniques for peptide detection and quantification. Its stability and defined mass-to-charge ratio make it suitable for use in chromatographic and spectrometric assays, where it can be employed to optimize separation conditions, evaluate detector response, and establish method sensitivity for short-chain peptides.
Nutritional biochemistry modeling: In studies simulating digestive or absorptive processes, lysyl-isoleucine can act as a model substrate to investigate peptide transport mechanisms across biological membranes. Researchers use it to examine the activity of peptide transporters, such as those in the intestinal epithelium, and to explore the influence of sequence composition on uptake efficiency. Insights gained from such experiments contribute to a deeper understanding of peptide absorption and metabolism in nutritional science.
By supporting research across enzymology, peptide chemistry, protein interaction analysis, analytical method development, and nutritional modeling, lysyl-isoleucine stands as a versatile tool for advancing knowledge in peptide-related biochemistry. Its defined structure and functional diversity enable precise experimental design and reliable data generation in a range of scientific applications.
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