Pro-Tyr connects turn-inducing proline with an aromatic tyrosine side chain, creating a dipeptide suited for β-turn and π-interaction studies. Backbone rigidity from proline shapes local structure, while tyrosine offers spectroscopic and hydrogen-bonding capabilities. Researchers examine its conformational ensembles in different solvents. Applications include motif design, enzyme-recognition modeling, and folding analysis.
CAT No: R2385
CAS No:19786-36-8
Synonyms/Alias:H-Pro-Tyr-OH;19786-36-8;Prolyl-tyrosine;Pro-tyr;L-Tyrosine, L-prolyl-;L-prolyl-L-tyrosine;N-L-prolyl-L-tyrosine;L-Pro-L-Tyr;L-Prolyl-L-tyrosine monohydrate;CHEBI:74799;L-Tyrosine, N-L-prolyl-;prolyltyrosine;(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-pyrrolidine-2-carbonyl]amino]propanoic acid;DTXSID30173493;Pro-Tyr-OH;PY dipeptide;P-Y Dipeptide;(S)-3-(4-Hydroxyphenyl)-2-((S)-pyrrolidine-2-carboxamido)Propanoic acid;(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-pyrrolidin-1-ium-2-carbonyl]amino]propanoate;Proline Tyrosine dipeptide;Proline-Tyrosine dipeptide;2-((hydroxy(pyrrolidin-2-yl)methylidene)amino)-3-(4-hydroxyphenyl)propanoate;2-{[hydroxy(pyrrolidin-2-yl)methylidene]amino}-3-(4-hydroxyphenyl)propanoate;MFCD00037870;H-Pro-Tyr-OH, AldrichCPR;CHEMBL298979;SCHEMBL6367397;DTXCID8095984;AKOS010408836;AT17293;BS-21911;CS-0449347;Q27144910;
Pro-Tyr, also known as Prolyl-Tyrosine, is a dipeptide composed of the amino acids proline and tyrosine linked via a peptide bond. As a member of the dipeptide class, it serves as a valuable biochemical tool in peptide research, enzymology, and protein chemistry. Its unique structural features, combining the conformational rigidity of proline with the aromatic character of tyrosine, make it highly relevant for studies exploring peptide structure-function relationships, protease specificity, and peptide transport mechanisms. The presence of both a secondary amine and a phenolic side chain further enhances its utility in various experimental and analytical contexts within the life sciences.
Peptide synthesis research: Pro-Tyr is frequently utilized as a building block in the synthesis of longer, sequence-defined peptides. Its incorporation into peptide chains can influence the overall secondary structure due to the conformational constraints imposed by the proline residue, as well as the potential for aromatic interactions provided by tyrosine. Researchers exploit these properties to design peptides with tailored biological activity, stability, or receptor-binding profiles, supporting the development of novel biomolecules for fundamental studies or advanced applications in molecular biology.
Enzymatic substrate characterization: The dipeptide serves as a model substrate for investigating the specificity and catalytic mechanisms of proteolytic enzymes, particularly dipeptidyl peptidases and aminopeptidases. By monitoring the enzymatic hydrolysis of Pro-Tyr, scientists can elucidate substrate preferences, kinetic parameters, and inhibition profiles. Such studies are critical for understanding enzyme function in physiological and pathological processes, as well as for screening potential enzyme inhibitors in drug discovery research.
Peptide transporter studies: Prolyl-tyrosine is employed in the characterization of peptide transport systems, such as PEPT1 and PEPT2, which mediate the cellular uptake of di- and tripeptides. Its defined structure and physicochemical properties make it a suitable probe for quantifying transport efficiency, substrate competition, and transporter regulation in various cell types. These investigations contribute to a deeper understanding of nutrient absorption, drug delivery mechanisms, and the pharmacokinetics of peptide-based therapeutics.
Analytical method development: The compound is widely used as a reference standard or calibration compound in chromatographic and spectrometric assays designed to quantify peptides in biological samples. Its well-defined chemical composition and predictable behavior in separation techniques facilitate the validation of analytical methods, supporting accurate detection and quantification of peptide analytes in complex matrices such as plasma, tissue extracts, or fermentation broths.
Structural and conformational analysis: Due to the interplay between proline-induced rigidity and tyrosine's aromaticity, Pro-Tyr is an informative model for studying peptide folding, backbone dynamics, and intramolecular interactions. Researchers employ it in nuclear magnetic resonance (NMR), circular dichroism (CD), and other spectroscopic techniques to probe the impact of sequence context on peptide conformation. Insights gained from such analyses inform the rational design of peptides with desired structural and functional attributes for use in materials science, biotechnology, and basic research.
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