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, also known as Pro-His, is a dipeptide composed of the amino acids proline and histidine linked by a peptide bond. As a naturally occurring peptide fragment, it is frequently studied for its unique biochemical properties and its role in modulating physiological processes. With a structure that allows for notable stability and reactivity, Prolyl-Histidine has attracted significant attention in the field of peptide research, particularly owing to its ability to interact with various enzymes and receptors. Its amphiphilic nature and capacity for hydrogen bonding make it a valuable tool in both fundamental and applied scientific studies, serving as a model compound for understanding peptide interactions and mechanisms in complex biological systems.
Peptide Enzyme Substrate Studies: In enzymology, Pro-His is often employed as a model substrate for investigating the specificity and catalytic mechanisms of dipeptidyl peptidases and other proteolytic enzymes. Researchers utilize this dipeptide to probe the enzyme's active site preferences, substrate recognition patterns, and cleavage processes. By analyzing how enzymes interact with Prolyl-Histidine, scientists can elucidate the structural and functional determinants of enzyme-substrate affinity, which is essential for the rational design of enzyme inhibitors or modified peptides with tailored activities. Such studies contribute to a deeper understanding of protein digestion, peptide turnover, and the regulation of peptide-mediated signaling pathways.
Antioxidant Mechanism Investigations: Prolyl-Histidine serves as a valuable probe in antioxidant research due to the presence of the imidazole ring in the histidine residue, which is known for its radical scavenging abilities. Experimental models frequently utilize this dipeptide to assess its efficacy in neutralizing reactive oxygen species and mitigating oxidative stress at the molecular level. By incorporating Pro-His into in vitro or cell-based assays, investigators can analyze its capacity to modulate redox balance, stabilize free radicals, and protect biomolecules from oxidative damage. Insights gained from these studies advance the understanding of peptide-based antioxidant mechanisms and support the development of novel antioxidant agents for a variety of research applications.
Peptide Transport and Absorption Research: The absorption and transport of small peptides like Prolyl-Histidine across biological membranes are critical topics in nutritional and pharmacological science. This dipeptide is frequently used to study the mechanisms of peptide uptake via specific transporters, such as PEPT1, in intestinal epithelial cells. Researchers employ Pro-His in uptake assays to characterize transporter specificity, kinetics, and regulation under different physiological and experimental conditions. These investigations are instrumental in deciphering how dietary peptides are absorbed in the gut, influencing nutrient bioavailability and the design of peptide-based delivery systems for improved oral bioactivity.
Metal Ion Chelation and Coordination Chemistry: The histidine residue in Prolyl-Histidine confers a strong affinity for binding divalent metal ions, making it an excellent candidate for metal chelation studies. Scientists utilize this peptide to explore its coordination behavior with metals such as copper, zinc, and nickel, both in solution and in model biological systems. By examining the binding interactions, stoichiometry, and stability constants, researchers gain valuable insights into the role of peptide-metal complexes in biological catalysis, metal homeostasis, and the prevention of metal-induced oxidative stress. Such studies are foundational for advancing metalloprotein research and the design of peptide-based chelators for analytical and biotechnological applications.
Peptide Structure-Activity Relationship (SAR) Analysis: Prolyl-Histidine is frequently incorporated into structure-activity relationship studies to investigate how sequence, conformation, and side-chain properties influence peptide function. By systematically modifying the dipeptide or comparing it with related analogs, researchers can delineate the key structural features that govern its biological activity, stability, and interaction with target molecules. These SAR investigations are critical for guiding the rational design of novel peptides with enhanced bioactivity, selectivity, or stability, thereby accelerating the development of next-generation peptide tools for research, diagnostics, and industrial applications.
Bioanalytical Method Development: Analytical chemists often employ Pro-His as a reference standard or model analyte in the development and validation of peptide detection and quantification methods. Its well-characterized structure and physicochemical properties make it suitable for optimizing chromatographic separation, mass spectrometric analysis, and sample preparation protocols. By utilizing this dipeptide in method development, laboratories can ensure robust, sensitive, and reproducible detection of similar peptides in complex biological matrices, thereby supporting high-quality analytical workflows in peptide research and quality control.
1. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
2. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
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