Phe-Lys aligns an aromatic phenylalanine with a basic lysine side chain, generating a dipeptide that models π-cation interactions. Hydrophobic and charged surfaces coexist, making it a useful probe for binding-pocket mapping. Researchers examine its conformational ensembles and solvent effects. Applications span peptide-receptor docking studies, enzymatic-specificity assays, and fundamental folding research.
CAT No: R2359
CAS No:6456-72-0
Synonyms/Alias:phenylalanyllysine;Phe-Lys;L-Phenylalanyl-L-Lysine;Phenylalanyl-Lysine;6456-72-0;FK dipeptide;F-K Dipeptide;L-Phe-L-Lys-OH;Phenylalanine Lysine dipeptide;CHEBI:141443;(2S)-6-amino-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]hexanoic acid;(2S)-6-Amino-2-(((2S)-2-amino-3-phenylpropanoyl)amino)hexanoate;(2S)-6-Amino-2-{[(2S)-2-amino-3-phenylpropanoyl]amino}hexanoate;6-Amino-2-((2-amino-1-hydroxy-3-phenylpropylidene)amino)hexanoate;6-Amino-2-[(2-amino-1-hydroxy-3-phenylpropylidene)amino]hexanoate;(2S)-6-amino-2-{[(2S)-2-amino-3-phenylpropanoyl]amino}hexanoic acid;6-amino-2-((2-amino-1-hydroxy-3-phenylpropylidene)amino)hexanoic acid;6-amino-2-[(2-amino-1-hydroxy-3-phenylpropylidene)amino]hexanoic acid;phenylalanyl-l-lysine;L-Phe-L-Lys;N2-Phenylalanyllysine;N2-L-Phenylalanyl-L-lysine;Phenylalanine-Lysine dipeptide;SCHEMBL170652;FK;F-K;
Phe-Lys, also known as Phenylalanyl-Lysine, is a synthetic dipeptide composed of the amino acids phenylalanine and lysine linked by a peptide bond. As a representative member of the dipeptide class, it exhibits unique physicochemical properties that make it a valuable tool in biochemical and molecular biology research. The arrangement of a hydrophobic aromatic residue (phenylalanine) with a basic, positively charged residue (lysine) in a single molecule allows for the study of sequence-dependent peptide behavior, intermolecular interactions, and structure-activity relationships. Its defined composition and stability further enhance its utility in experimental systems exploring peptide function, transport, and metabolism.
Peptide transport studies: Phe-Lys serves as a model substrate for investigating the mechanisms of peptide transport across biological membranes. Its structure allows researchers to probe the specificity and kinetics of peptide transporters such as PEPT1 and PEPT2 in both prokaryotic and eukaryotic systems. By utilizing this dipeptide, scientists can dissect the influence of side-chain characteristics on transporter affinity and elucidate the molecular determinants governing dipeptide uptake, which is critical for understanding nutrient absorption and drug delivery strategies involving peptide mimetics.
Enzymatic hydrolysis assays: The dipeptide is frequently used in enzymology to assess the substrate specificity and catalytic efficiency of various proteases and peptidases. Due to the distinct chemical properties of its constituent amino acids, Phe-Lys provides a means to analyze endopeptidase and exopeptidase activity, enabling the characterization of enzyme substrate preferences and reaction mechanisms. Such assays contribute to the development of enzyme inhibitors and the broader understanding of proteolytic pathways in physiological and industrial contexts.
Peptide synthesis validation: As a well-characterized dipeptide, Phe-Lys is commonly employed as a standard or reference compound in the validation of peptide synthesis protocols. Its defined sequence and analytical tractability make it suitable for calibrating chromatographic systems, optimizing purification methods, and benchmarking the performance of solid-phase peptide synthesis (SPPS) techniques. This application supports quality control and process development in research laboratories and peptide manufacturing settings.
Structural and conformational studies: The combination of an aromatic and a basic residue in Phe-Lys provides a valuable framework for exploring peptide secondary structure formation and side-chain interactions. Researchers utilize it to investigate the influence of sequence context on peptide folding, aggregation, and intermolecular binding. Insights gained from such studies inform the rational design of bioactive peptides, peptide-based materials, and molecular probes for diverse scientific fields.
Analytical method development: The dipeptide is also utilized in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its physicochemical properties, including charge, hydrophobicity, and UV absorbance, render it an effective analyte for optimizing separation parameters and sensitivity in peptide quantification workflows. These applications are essential for advancing analytical capabilities in proteomics, pharmaceutical analysis, and quality assurance processes.
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