Pro-Lys is a dipeptide combining a conformationally restricted proline with a basic lysine side chain. Researchers use it to study peptide bending, electrostatic influences, and backbone mobility. The motif supports exploration of β-turn behavior and ligand-binding contributions. Its compact structure facilitates controlled mechanistic analysis.
CAT No: R2315
CAS No:71227-70-8
Synonyms/Alias:Pro-Lys;L-Prolyl-L-lysine;H-Pro-Lys-OH;Prolyl-Lysine;71227-70-8;L-Pro-L-Lys;CHEBI:74792;(2S)-6-amino-2-[[(2S)-pyrrolidine-2-carbonyl]amino]hexanoic Acid;H-Pro-Lys-OHacetatesalt;CHEMBL377325;PK dipeptide;P-K Dipeptide;H-PRO-LYS-OH ACETATE SALT;Proline Lysine dipeptide;Proline-Lysine dipeptide;(2S)-6-amino-2-(((2S)-pyrrolidine-2-carbonyl)amino)hexanoic acid;6-Amino-2-((hydroxy(pyrrolidin-2-yl)methylidene)amino)hexanoate;6-Amino-2-{[hydroxy(pyrrolidin-2-yl)methylidene]amino}hexanoate;SCHEMBL18075734;HY-P4558;BDBM50188505;FP108159;CS-0655117;Q27144903;
Pro-Lys, also known as prolyl-lysine, is a synthetic dipeptide composed of the amino acids proline and lysine linked via a peptide bond. As a member of the peptide compound category, it serves as a valuable model system for investigating peptide structure, function, and reactivity. Its unique combination of a cyclic imino acid and a basic, ε-amino group-containing residue makes it particularly relevant for studies exploring peptide folding, intermolecular interactions, and the influence of specific side chains on biochemical processes. The presence of both hydrophobic and charged moieties within Pro-Lys provides researchers with a versatile tool for probing sequence-dependent behaviors in peptides and proteins, as well as for supporting method development in peptide chemistry.
Peptide synthesis research: In the field of synthetic peptide chemistry, Pro-Lys is frequently used as a model dipeptide to optimize and validate coupling strategies, deprotection protocols, and purification workflows. Its defined sequence allows for the assessment of synthetic efficiency and the identification of potential side reactions, particularly those involving the secondary amine of proline or the basic side chain of lysine. By incorporating this dipeptide into test reactions, researchers can benchmark the performance of reagents, resins, and analytical techniques, thereby improving the reliability and reproducibility of solid-phase and solution-phase peptide synthesis.
Protein structure and folding studies: The combination of proline, which introduces conformational constraints, and lysine, which contributes a flexible, charged side chain, makes Pro-Lys a useful probe for examining sequence-specific effects on peptide backbone dynamics and secondary structure formation. Scientists utilize this dipeptide to investigate how proline-induced kinks and lysine-mediated electrostatic interactions influence the folding, stability, and aggregation propensity of larger peptides and proteins. Such studies provide insight into the fundamental principles governing protein architecture and misfolding-related phenomena.
Enzyme substrate specificity assays: Pro-Lys serves as a convenient substrate or inhibitor in assays designed to characterize the specificity and catalytic mechanisms of proteases, peptidases, and other peptide-modifying enzymes. Its defined sequence enables precise mapping of enzyme recognition sites and cleavage preferences, facilitating the identification of substrate determinants and the development of selective enzyme inhibitors. The dipeptide's utility in these assays supports both basic enzymology and the screening of compound libraries for modulators of proteolytic activity.
Analytical method development: In analytical biochemistry, Pro-Lys is employed as a standard or reference compound for the calibration and validation of chromatographic, electrophoretic, and mass spectrometric techniques. Its physicochemical properties, including charge, hydrophobicity, and molecular weight, make it suitable for testing the resolution, sensitivity, and reproducibility of peptide analysis workflows. Utilizing this dipeptide as a benchmark can aid in the optimization of separation parameters and detection protocols, ensuring accurate quantification and characterization of peptide samples.
Peptide interaction and binding studies: Due to its bifunctional nature, Pro-Lys is valuable for probing intermolecular interactions, such as peptide-peptide association, peptide-ligand binding, or peptide-membrane affinity. Researchers use it to explore how sequence context and side chain properties influence binding affinities and specificities, which is critical for understanding molecular recognition events in biological systems. The dipeptide's well-defined structure enables systematic variation in experimental design, supporting the elucidation of binding mechanisms and the development of peptide-based probes or affinity reagents.
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