Histidyltyrosine is a novel enhancer of catalytic efficiency of neurolysin.
CAT No: 10-101-276
CAS No:35979-00-1
Synonyms/Alias:H-HIS-TYR-OH;35979-00-1;His-Tyr;L-histidyl-L-tyrosine;CHEBI:74059;HY dipeptide;histidyl-tyrosine;Histidinyltyrosine;H-Y Dipeptide;histidyltyrosine;L-Histidinyl-L-Tyrosine;Histidine Tyrosine dipeptide;Histidine-Tyrosine dipeptide;(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid;CHEMBL3321987;(S)-2-((S)-2-Amino-3-(1H-imidazol-4-yl)Propanamido)-3-(4-hydroxyphenyl)Propanoic acid;Histidinyl-Tyrosine;L-Tyrosine, L-histidyl-;N-L-Histidyl-L-tyrosine;N-Histidyltyrosine;(2S)-2-(((2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl)amino)-3-(4-hydroxyphenyl)propanoic acid;(2S)-2-(((2S)-2-azaniumyl-3-(1H-imidazol-5-yl)propanoyl)amino)-3-(4-hydroxyphenyl)propanoate;(2S)-2-[[(2S)-2-azaniumyl-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(4-hydroxyphenyl)propanoate;N-Histidinyltyrosine;MFCD00037859;L-His-L-Tyr;N-L-Histidinyl-L-tyrosine;SCHEMBL1985387;SCHEMBL21828646;HTOOKGDPMXSJSY-STQMWFEESA-N;HY;BDBM50049710;AKOS028113082;BS-16656;FH108070;CS-0149668;D81943;Q27144372;
H-His-Tyr-OH, also known as L-Histidyl-L-Tyrosine, is a synthetic dipeptide composed of the amino acids histidine and tyrosine linked through a peptide bond. This compound is highly valued in biochemical research for its unique structural features, which combine the imidazole side chain of histidine and the phenolic group of tyrosine. Such a combination provides distinctive chemical reactivity and potential for participation in various molecular interactions. As a result, H-His-Tyr-OH serves as a versatile model in studies seeking to understand peptide behavior, enzyme-substrate specificity, and the physicochemical properties of short peptide sequences. Its solubility and stability under different experimental conditions further make it an attractive choice for laboratory investigations and method development.
Peptide Structure-Activity Relationship Studies: H-His-Tyr-OH is frequently employed in structure-activity relationship (SAR) studies, where its dipeptide framework helps elucidate how modifications in peptide sequences influence biological activity and molecular recognition. By analyzing the interaction of this dipeptide with enzymes or receptors, researchers can gain insights into the roles played by histidine and tyrosine residues in protein-ligand binding, as well as the contribution of their side chains to the overall peptide conformation and reactivity. Such findings are instrumental in guiding the rational design of novel peptides with tailored properties for research or industrial purposes.
Enzyme Substrate Specificity Assays: As a model substrate, L-Histidyl-L-Tyrosine is widely used in enzymology to investigate the specificity and catalytic mechanisms of various proteases and peptidases. Its defined sequence allows researchers to monitor enzymatic cleavage patterns and to study the influence of adjacent amino acids on enzyme selectivity. These assays contribute to a deeper understanding of peptide processing and degradation, which is essential for mapping metabolic pathways and for the development of enzyme inhibitors.
Peptide Synthesis Method Development: The dipeptide H-His-Tyr-OH is often utilized in the optimization and validation of peptide synthesis protocols, especially in solid-phase peptide synthesis (SPPS). Its dual functional groups present challenges in coupling and deprotection steps, making it a valuable test case for evaluating new reagents, protecting group strategies, and purification methods. By refining these techniques using this dipeptide, researchers can improve the efficiency and yield of more complex peptide syntheses, benefiting both academic and industrial laboratories.
Analytical Method Calibration: In the field of analytical chemistry, L-Histidyl-L-Tyrosine serves as a standard for calibrating and validating chromatographic and spectrometric methods designed to detect and quantify peptides. Its well-characterized properties enable accurate assessment of method sensitivity, linearity, and reproducibility. The use of this dipeptide in method development ensures reliable detection of similar compounds in complex biological or synthetic samples, supporting high-quality data generation in peptide research.
Biophysical and Structural Analysis: H-His-Tyr-OH is also instrumental in biophysical studies aimed at understanding peptide folding, aggregation, and intermolecular interactions. Its simple yet functionally diverse structure allows for detailed investigations using techniques such as NMR spectroscopy, circular dichroism, and mass spectrometry. These analyses provide valuable information on the conformational preferences and stability of short peptides, informing broader research into protein folding disorders, peptide-based materials, and molecular recognition processes. By leveraging the unique features of this dipeptide, scientists can explore fundamental aspects of peptide chemistry and apply their findings to diverse areas of biochemical and pharmaceutical research.
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