Prolyl-Histidine is a dipeptide combining conformationally restricted proline with an imidazole-bearing histidine. The sequence is valuable for exploring pH-dependent coordination and proton-transfer mechanisms. Researchers analyze its ability to bind metal ions and stabilize specific backbone geometries. Applications include catalyst-mimetic systems, histidine-motif studies, and structural modeling.
CAT No: R2388
CAS No:92027-43-5
Synonyms/Alias:Prolyl-Histidine;92027-43-5;L-Histidine, L-prolyl-;N-L-Prolyl-L-histidine;(2S)-3-(1H-imidazol-5-yl)-2-[[(2S)-pyrrolidine-2-carbonyl]amino]propanoic acid;(S)-3-(1H-Imidazol-4-yl)-2-((S)-pyrrolidine-2-carboxamido)propanoic acid;L-Prolyl-L-Histidine;N-prolyl histidine;SCHEMBL18048894;CHEBI:157883;AKOS010421287;(2S)-3-(1H-imidazol-5-yl)-2-{[(2S)-pyrrolidin-2-yl]formamido}propanoic acid;
Prolyl-Histidine is a synthetic dipeptide composed of the amino acids proline and histidine linked via a peptide bond. As a member of the dipeptide class, it offers a unique combination of the structural rigidity of proline and the imidazole functionality of histidine, making it relevant for a variety of biochemical and biophysical investigations. Its sequence, reflecting naturally occurring motifs found in proteins and bioactive peptides, has attracted interest in research focused on peptide structure-function relationships, enzymatic specificity, and peptide-based modulation of biological processes. The compound's physicochemical properties and defined sequence enable its use as a model substrate, analytical standard, and building block in diverse peptide research contexts.
Peptide Structure-Activity Studies: The dipeptide serves as a valuable tool for elucidating the influence of specific amino acid arrangements on peptide conformation and biological activity. By incorporating proline, which induces kinks or turns in peptide chains, alongside histidine, known for its metal-binding and catalytic properties, researchers can dissect how such motifs affect protein folding, stability, and interaction with other biomolecules. These studies contribute to a deeper understanding of the relationship between primary sequence and functional behavior in peptides and proteins.
Enzymatic Substrate Analysis: Prolyl-Histidine is frequently employed as a model substrate in enzymology, particularly for assessing the specificity and catalytic mechanisms of peptidases, including dipeptidyl peptidases and aminopeptidases. Its defined sequence allows for precise monitoring of enzymatic cleavage, facilitating kinetic studies and inhibitor screening. Such applications are critical for characterizing enzyme-substrate interactions, mapping active sites, and developing enzyme modulators for research purposes.
Analytical Method Development: The compound is useful as a standard or calibration reference in analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its well-characterized properties support method validation, system suitability testing, and quantification of peptide analytes in complex mixtures. Employing this dipeptide in analytical workflows enhances the reliability and reproducibility of peptide detection and quantification in research and quality control laboratories.
Peptide Synthesis Optimization: In synthetic peptide chemistry, prolyl-containing sequences are often challenging due to the conformational constraints imposed by proline. Prolyl-Histidine serves as a representative model for optimizing coupling strategies, protecting group schemes, and purification methods in solid-phase peptide synthesis (SPPS) and solution-phase protocols. Insights gained from its synthesis and purification inform best practices for assembling more complex peptides and peptidomimetics.
Biophysical Characterization: The dipeptide provides a tractable system for investigating fundamental aspects of peptide solubility, aggregation, and interaction with metal ions or small molecules. Studies utilizing this compound can reveal how short peptide sequences behave under varying pH, ionic strength, or in the presence of cofactors, informing the design of peptide-based materials and probes. Such biophysical analyses contribute to the broader field of peptide science, supporting the development of novel applications in research and industry.
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