H-Lys-Leu-Val-Phe-Phe-OH combines hydrophobic and aromatic residues with a basic N-terminal lysine that modulates solubility and binding. The sequence supports investigations of π-stacking and hydrophobic packing. Researchers explore its folding preferences in solution. Use extends to motif analysis, peptide design, and binding-model studies.
CAT No: R2448
CAS No:153247-40-6
Synonyms/Alias:h-lys-leu-val-phe-phe-oh;153247-40-6;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-4-methylpentanoyl]amino]-3-methylbutanoyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoic acid;Amyloid b-Protein (16-20);Lys-Leu-Val-Phe-Phe;L-Phenylalanine,L-lysyl-L-leucyl-L-valyl-L-phenylalanyl-;HY-P5124;FA109060;CS-0774329;Amyloid beta-Protein (16-20) trifluoroacetate salt;
h-Lys-leu-val-phe-phe-oh, also known as a synthetic pentapeptide, represents a valuable tool for researchers exploring the intricate roles of short-chain peptides in biological systems. Characterized by its unique sequence of lysine, leucine, valine, and two phenylalanine residues, this compound offers a versatile platform for investigating protein-protein interactions, receptor binding dynamics, and peptide structure-activity relationships. Its defined structure enables precise experimental manipulations, making it a preferred choice for studies requiring consistent and reproducible results. With its capacity for customization, h-Lys-leu-val-phe-phe-oh facilitates the development of novel peptide-based probes, allowing for the elucidation of complex biochemical pathways and the advancement of peptide engineering strategies.
Peptide-Protein Interaction Studies: In the field of molecular biology, h-Lys-leu-val-phe-phe-oh is frequently employed to dissect the mechanisms underlying specific peptide-protein interactions. By serving as a model ligand, it allows researchers to map binding sites, measure binding affinities, and analyze the conformational changes induced upon complex formation. Such studies are crucial for understanding the fundamental principles governing cellular signaling, enzyme regulation, and the modulation of protein function by bioactive peptides. The pentapeptide's modularity also supports the design of analogues to probe structure-function relationships, thereby expanding the knowledge base required for rational peptide design.
Receptor Binding Assays: Synthetic peptides like h-Lys-leu-val-phe-phe-oh are instrumental in receptor binding assays, where they are used to simulate endogenous peptide ligands and evaluate receptor specificity and affinity. Through radiolabeled or fluorescently labeled versions, researchers can quantify binding kinetics, investigate competitive inhibition, and characterize novel receptor subtypes. These assays play a pivotal role in pharmacological research by informing the identification of new molecular targets and facilitating the screening of candidate compounds that may modulate receptor-mediated pathways.
Peptide Structural Analysis: The defined sequence of h-Lys-leu-val-phe-phe-oh makes it an ideal substrate for structural studies using techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD) spectroscopy, and X-ray crystallography. By analyzing its three-dimensional conformation in solution or crystalline form, scientists can gain insights into peptide folding, secondary structure formation, and the influence of side-chain interactions. Such information is essential for the rational design of peptidomimetics and for understanding the structural determinants of peptide stability and bioactivity.
Biochemical Pathway Elucidation: The application of h-Lys-leu-val-phe-phe-oh extends to the investigation of complex biochemical pathways, where it can act as a substrate, inhibitor, or modulator of enzymatic reactions. By monitoring the peptide's metabolic fate or its effect on specific enzymes, researchers can unravel the steps involved in peptide processing, degradation, and signal transduction. This approach is particularly valuable for mapping protease specificity and for identifying regulatory checkpoints in peptide-mediated signaling cascades.
Peptide Engineering and Modification: In the realm of peptide engineering, h-Lys-leu-val-phe-phe-oh serves as a foundational scaffold for the synthesis of modified peptides with enhanced properties. By introducing chemical modifications such as cyclization, side-chain functionalization, or conjugation to other biomolecules, scientists can tailor its activity, stability, and target specificity. These engineered peptides are subsequently evaluated for their potential as molecular probes, research tools, or building blocks in the development of innovative biomaterials. Through its multifaceted applications, h-Lys-leu-val-phe-phe-oh continues to drive progress in peptide science, supporting the discovery of new molecular mechanisms and the creation of advanced research reagents.
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