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 is a synthetic hexapeptide composed of the amino acid sequence lysine-lysine-proline-tyrosine-isoleucine-leucine, featuring a free carboxyl terminus. As a custom peptide, it serves as a versatile tool in biochemical research, enabling the study of sequence-specific interactions, structure-activity relationships, and peptide-driven cellular processes. Its defined sequence and modularity make it suitable for a range of investigative applications, particularly in the exploration of protein-protein interactions, enzymatic specificity, and receptor binding dynamics. The presence of both basic and hydrophobic residues within its sequence further enhances its utility for probing molecular recognition events and conformational properties relevant to peptide science.
Peptide structure-function analysis: Researchers utilize this hexapeptide as a model system to elucidate the relationship between primary sequence and higher-order structure. By subjecting the peptide to biophysical characterization methods such as circular dichroism spectroscopy or nuclear magnetic resonance, scientists can investigate how specific amino acid arrangements influence secondary structure formation, stability, and folding propensity. Such insights are valuable for designing novel peptides with tailored biological or physicochemical properties.
Enzyme substrate studies: The sequence of this peptide provides a suitable substrate for investigating proteolytic activity and specificity of various peptidases and proteases. By monitoring the cleavage patterns and kinetics in enzymatic assays, researchers can gain a deeper understanding of substrate recognition, active site preferences, and catalytic efficiency. This information is crucial for mapping enzyme specificity profiles, screening for potential inhibitors, or validating enzymatic function in biochemical pathways.
Protein-protein interaction mapping: Owing to its well-defined sequence, the hexapeptide can be employed in binding assays to probe interactions with target proteins, antibodies, or other biomolecules. Surface plasmon resonance, isothermal titration calorimetry, or pull-down experiments can be performed to quantify binding affinities and delineate interaction interfaces. These studies are instrumental in identifying key residues involved in molecular recognition and in developing peptide-based affinity reagents or inhibitors.
Peptide-based assay development: The hexapeptide serves as a modular component in the design of biochemical assays, such as fluorescence-based detection systems or competitive binding formats. By incorporating suitable tags or labels, it can be used to monitor biological processes, screen for modulators of peptide-protein interactions, or validate the activity of signaling molecules. The flexibility in sequence modification further allows adaptation to specific assay requirements, supporting high-throughput screening and mechanistic studies.
Synthetic peptide standardization: In peptide synthesis laboratories, this compound functions as a reference standard for validating solid-phase peptide synthesis protocols and analytical methods. Its defined sequence and physicochemical properties enable calibration of chromatographic systems, mass spectrometric analysis, and quality control procedures. Consistent use of such standards ensures reproducibility and accuracy in peptide production workflows, supporting both research and development activities in peptide chemistry.
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