Lysyl-Isoleucine

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.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Lysyl-Isoleucine(CAS 20556-13-2)

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;

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M.F/Formula
C12H25N3O3
M.W/Mr.
259.35
Sequence
One Letter Code:KI
Three Letter Code:H-Lys-Ile-OH

Lysyl-Isoleucine, also known as Lys-Ile, is a dipeptide composed of the amino acids lysine and isoleucine linked by a peptide bond. This compound is synthesized through controlled peptide coupling techniques, resulting in a molecule that combines the distinct physicochemical properties of both constituent amino acids. Owing to its unique structural configuration, Lysyl-Isoleucine exhibits enhanced solubility and stability compared to its free amino acid components. Its amphiphilic nature makes it a valuable tool in various biochemical and molecular biology applications, particularly where the interplay between hydrophilic and hydrophobic interactions is crucial. The presence of both a basic side chain from lysine and a branched aliphatic side chain from isoleucine allows for versatile interactions within peptide-based systems, thus broadening its utility in research and development.

Peptide synthesis research: Lysyl-Isoleucine serves as a fundamental building block in the synthesis of longer peptides and proteins in solid-phase peptide synthesis protocols. Researchers utilize this dipeptide to introduce specific sequence motifs that can influence the overall folding, stability, and biological activity of synthetic peptides. Its incorporation can be strategically chosen to manipulate the physicochemical properties of the resulting peptide, such as charge distribution and hydrophobicity, which are critical for mimicking natural protein structures or designing novel bioactive peptides. By providing a reliable and consistent dipeptide unit, Lys-Ile streamlines the assembly process, reduces potential racemization, and enhances the efficiency of peptide chain elongation.

Protein engineering studies: In the field of protein engineering, Lysyl-Isoleucine is employed to investigate the effects of dipeptide insertions or substitutions on protein structure and function. Its dual characteristics allow scientists to explore how the introduction of basic and hydrophobic residues in close proximity can modulate protein folding pathways, stability, and intermolecular interactions. The use of Lys-Ile in mutagenesis experiments facilitates the systematic study of sequence-structure-function relationships, enabling the rational design of proteins with tailored properties for industrial, analytical, or therapeutic applications.

Enzyme substrate specificity assays: Researchers leverage Lysyl-Isoleucine as a model substrate in enzymology to probe the specificity and catalytic mechanisms of proteases and peptidases. By monitoring the enzymatic cleavage of this dipeptide, scientists can gain insights into enzyme recognition motifs and substrate preferences, which are vital for elucidating enzyme function and for screening potential enzyme inhibitors. The distinct side chains of lysine and isoleucine provide a useful contrast in substrate profiling, aiding in the differentiation of enzyme subtypes and in the characterization of novel catalytic activities.

Biomaterials development: The amphiphilic nature of Lysyl-Isoleucine is exploited in the design and fabrication of peptide-based biomaterials. Its incorporation into self-assembling peptide systems can modulate the mechanical properties, surface charge, and biocompatibility of hydrogels, nanofibers, or coatings. Researchers utilize Lys-Ile to tune the interactions between peptide chains, thereby influencing the morphological and functional characteristics of the resulting biomaterial. Such materials find application in tissue engineering, cell culture scaffolds, and as carriers for bioactive molecules, where precise control over material properties is essential.

Analytical method development: Analytical chemists employ Lysyl-Isoleucine as a standard or reference compound in chromatographic and mass spectrometric techniques. Its well-defined structure and predictable behavior under various analytical conditions make it an ideal candidate for method calibration, validation, and quantification of peptide-related analytes. The presence of both a basic and a hydrophobic residue facilitates its detection and separation, providing a robust tool for evaluating the performance of analytical platforms designed to analyze peptides and proteins.

Peptide-based drug delivery research: Lysyl-Isoleucine is investigated for its potential role in the development of peptide-based delivery systems. Its structural features enable the design of conjugates or carriers that can enhance the solubility, stability, and cellular uptake of therapeutic agents. By incorporating Lys-Ile into delivery vectors, researchers aim to optimize the pharmacokinetic properties and target specificity of peptide-based formulations. This approach supports the advancement of innovative strategies for the efficient and controlled delivery of bioactive molecules, contributing to the expanding field of peptide therapeutics and nanomedicine.

InChI
InChI=1S/C12H25N3O3/c1-3-8(2)10(12(17)18)15-11(16)9(14)6-4-5-7-13/h8-10H,3-7,13-14H2,1-2H3,(H,15,16)(H,17,18)/t8-,9-,10-/m0/s1
InChI Key
FMIIKPHLJKUXGE-GUBZILKMSA-N

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