H-Lys-lys-pro-tyr-ile-leu-OH is a hexapeptide combining basic, aromatic, and hydrophobic residues that influence β-turn formation and packing interactions. Researchers use it to study electrostatic modulation, solvent-dependent folding, and ligand-binding motifs. The sequence's polarity profile supports high-resolution conformational assays. Its accessible termini facilitate synthetic modification.
CAT No: R2404
CAS No:139026-64-5
Synonyms/Alias:H-LYS-LYS-PRO-TYR-ILE-LEU-OH;139026-64-5;[Lys8, Lys9]-Neurotensin (8-13);CHEMBL258221;(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2,6-diaminohexanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoic acid;JMV438;(Lys8,lys9)-neurotensin(8-13);HY-P2544;BDBM50342242;AKOS040756716;NCGC00167231-01;MS-31355;CS-0135088;G12531;(S)-2-((2S,3S)-2-((S)-2-((S)-1-((S)-6-amino-2-((S)-2,6-diaminohexanamido)hexanoyl)pyrrolidine-2-carboxamido)-3-(4-hydroxyphenyl)propanamido)-3-methylpentanamido)-4-methylpentanoic acid;
H-Lys-lys-pro-tyr-ile-leu-OH, also known as a hexapeptide with the sequence Lys-Lys-Pro-Tyr-Ile-Leu, is a synthetic peptide compound that has garnered significant attention in biochemical and life science research. Characterized by its unique arrangement of amino acids, this peptide exhibits properties that make it a valuable tool for investigating protein interactions, cellular signaling pathways, and enzymatic activity. Its structure, featuring two lysine residues at the N-terminus, imparts a basic character that can influence molecular recognition and binding affinity. Researchers utilize this peptide in a variety of experimental systems, leveraging its stability and versatility to explore fundamental questions in molecular biology, biochemistry, and peptide engineering.
Peptide-Protein Interaction Studies: H-Lys-lys-pro-tyr-ile-leu-OH serves as a model peptide for studying the dynamics of peptide-protein interactions in vitro. Its specific sequence allows scientists to investigate how basic residues, proline-induced conformational constraints, and aromatic side chains contribute to binding specificity and affinity. By incorporating this hexapeptide into surface plasmon resonance or isothermal titration calorimetry assays, researchers can dissect the thermodynamics and kinetics of molecular recognition events, providing insights into the underlying mechanisms that govern protein-ligand interactions in biological systems.
Enzyme Substrate Analysis: The hexapeptide is frequently employed as a substrate in enzymatic assays to evaluate protease specificity and activity. Its sequence, containing both basic and hydrophobic amino acids, makes it an excellent candidate for testing how different classes of proteases recognize and cleave peptide bonds. By monitoring the cleavage patterns of Lys-Lys-Pro-Tyr-Ile-Leu in vitro, enzymologists can elucidate substrate preferences, map active sites, and develop novel enzyme inhibitors for research applications.
Cell Signaling Pathway Research: Researchers utilize this synthetic peptide to probe cellular signaling pathways, particularly those involving receptor-mediated processes. The presence of tyrosine within the sequence enables phosphorylation studies, allowing scientists to mimic or investigate post-translational modifications that regulate signal transduction. By introducing the peptide into cell-based assays, it becomes possible to monitor downstream effects on kinase activity, receptor binding, and cellular responses, thus advancing our understanding of complex intracellular communication networks.
Peptide Structural Analysis: Lys-Lys-Pro-Tyr-Ile-Leu is also valuable in structural biology research, where it functions as a model system for studying peptide folding, stability, and secondary structure formation. The inclusion of proline, known for its conformational rigidity, provides an opportunity to examine how specific residues influence peptide backbone flexibility and overall three-dimensional architecture. Techniques such as nuclear magnetic resonance spectroscopy and circular dichroism spectroscopy are commonly applied to analyze the structural properties of this hexapeptide, yielding data that inform the design of novel peptides with tailored biophysical characteristics.
Antibody Epitope Mapping: In immunological research, this peptide sequence is used to identify and characterize antibody binding sites, or epitopes, on target proteins. By synthesizing and immobilizing Lys-Lys-Pro-Tyr-Ile-Leu on assay platforms, scientists can screen for antibody reactivity and map the regions responsible for immune recognition. This approach facilitates the development of more specific and effective antibodies for research and diagnostic purposes, while also contributing to the broader field of antigen-antibody interaction studies.
Peptide drug design and biomaterials research: Beyond fundamental research, H-Lys-lys-pro-tyr-ile-leu-OH finds utility in the early stages of peptide drug design and biomaterials development. Its defined sequence and physicochemical properties make it a template for designing analogs with improved stability, bioactivity, or targeted delivery capabilities. Additionally, incorporating this hexapeptide into polymeric scaffolds or hydrogels can enhance the biocompatibility and functionality of biomaterials intended for tissue engineering or regenerative medicine research. By serving as a starting point for rational design and functionalization, this peptide continues to expand its impact across multiple scientific disciplines, driving innovation and discovery in the fields of molecular biology, biochemistry, and material science.
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