LCKLSL is a N-terminal hexapeptide and a competitive annexin A2 (AnxA2) inhibitor. LCKLSL potently inhibits the binding of tissue plasminogen activator (tPA) to AnxA2. LCKLSL also inhibits the generation of plasmin and has anti-angiogenic roles.
CAT No: R1923
CAS No:533902-29-3
Synonyms/Alias:LCKLSL;533902-29-3;HY-P2333;AKOS040758181;CS-0130051;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2R)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-sulfanylpropanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoic acid;
LCKLSL is a synthetic peptide composed of the amino acid sequence Leu-Cys-Lys-Leu-Ser-Leu, designed for advanced research applications in biochemistry and molecular biology. As a short functional peptide, it offers a versatile tool for investigating peptide structure-activity relationships, protein interaction motifs, and signaling pathways. The sequence incorporates both hydrophobic and polar residues, making it suitable for studies of peptide folding, aggregation, and receptor binding. Its defined structure and ease of modification render it a valuable component for probing fundamental mechanisms in peptide science and for developing new peptide-based assays.
Peptide-protein interaction studies: LCKLSL serves as a model sequence for exploring the molecular basis of peptide-protein interactions. Researchers utilize it to characterize binding affinities, map interaction sites, and assess the influence of sequence modifications on target recognition. The presence of both hydrophobic and charged residues in the sequence enables investigations into how such motifs contribute to specificity and stability in peptide-mediated binding events, which is essential for understanding cellular communication and signal transduction processes.
Peptide synthesis optimization: The hexapeptide is frequently employed in method development and validation within solid-phase peptide synthesis (SPPS). Its sequence, which includes a cysteine residue, allows for the evaluation of strategies for disulfide bridge formation, side-chain protection, and peptide cleavage. By using this compound as a test substrate, synthetic chemists can refine protocols that minimize side reactions, improve yield, and enhance the purity of more complex peptide products, thereby advancing the efficiency and reliability of peptide manufacturing workflows.
Structural biology research: LCKLSL is utilized in conformational studies to elucidate the principles governing peptide folding and secondary structure formation. Its combination of leucine-rich hydrophobic stretches and polar residues makes it an effective model for examining helix propensity, beta-turn formation, and aggregation behavior in short peptides. Such studies contribute to the broader understanding of how primary sequence dictates higher-order structure, which is fundamental to protein engineering and the design of biomimetic materials.
Receptor binding assays: The defined sequence of this peptide enables its use as a probe in receptor binding experiments, where it can be labeled or modified to investigate ligand-receptor interactions. Researchers employ it to screen for binding partners, characterize affinity constants, and explore the effects of sequence alterations on biological activity. These studies are critical for identifying novel peptide ligands and for mapping the molecular determinants of receptor specificity in pharmacological and cell signaling research.
Analytical method development: In analytical chemistry, LCKLSL is adopted as a standard or calibration peptide for mass spectrometry and chromatographic techniques. Its well-characterized sequence and predictable physicochemical properties facilitate the establishment of detection limits, retention times, and fragmentation patterns. Such applications are vital for validating analytical platforms used in proteomics, quality control, and peptide quantification, ensuring reproducibility and accuracy in peptide analysis workflows.
2. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
4. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
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