Thr-Phe links a polar threonine to an aromatic phenylalanine, forming a dipeptide that models hydrogen bonding and π-interactions. The sequence aids exploration of helix nucleation and β-turn formation. Researchers assess its conformational ensemble and solvent dependence. Applications include peptide-folding studies, enzyme-substrate modeling, and design of minimal recognition motifs.
CAT No: R2574
CAS No:16875-27-7
Synonyms/Alias:H-Thr-Phe-OH;Thr-Phe;16875-27-7;threonylphenylalanine;L-THREONYL-L-PHENYLALANINE;CHEBI:74862;TF dipeptide;T-F Dipeptide;threonyl-phenylalanine;Threoninylphenylalanine;L-Threoninyl-L-Phenylalanine;CHEMBL3321993;Threonine Phenylalanine dipeptide;Threonine-Phenylalanine dipeptide;(S)-2-((2S,3R)-2-Amino-3-hydroxybutanamido)-3-phenylpropanoic acid;(2S)-2-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]-3-phenylpropanoic acid;N-Threonylphenylalanine;(2S)-2-(((2S,3R)-2-amino-3-hydroxybutanoyl)amino)-3-phenylpropanoic acid;(2S)-2-(((2S,3R)-2-amino-1,3-dihydroxybutylidene)amino)-3-phenylpropanoate;(2S)-2-{[(2S,3R)-2-amino-1,3-dihydroxybutylidene]amino}-3-phenylpropanoate;L-3-Phenyl-N-L-threonylalanine;N-L-Threonyl-L-phenylalanine;15: PN: EP2161028 PAGE: 10 Claimed Protein;;MFCD00038591;L-Thr-L-Phe;Threoninyl-Phenylalanine;N-Threoninylphenylalanine;H-Thr-Phe-OH, AldrichCPR;N-L-Threonyl-L-phenylalanine;SCHEMBL233445;N-L-Threoninyl-L-phenylalanine;(2S)-2-[(2S,3R)-2-AMINO-3-HYDROXYBUTANAMIDO]-3-PHENYLPROPANOIC ACID;DTXSID101346616;HY-P4626;BDBM50049727;FT108188;CS-0655422;Q27144972;
Thr-Phe, also known as Threonylphenylalanine, is a dipeptide composed of the amino acids threonine and phenylalanine linked by a single peptide bond. As a member of the peptide compound class, it serves as a valuable model for investigating peptide structure, function, and interactions in biochemical research. The presence of both a polar hydroxyl group from threonine and a hydrophobic aromatic ring from phenylalanine imparts unique physicochemical properties, making this dipeptide particularly relevant for studies involving peptide conformational dynamics, enzyme specificity, and transport mechanisms. Its defined sequence and manageable size allow for controlled experimentation in peptide-related research, supporting advancements in both fundamental and applied biochemical sciences.
Peptide structure-function analysis: Thr-Phe is frequently utilized as a model substrate in studies aimed at elucidating the relationship between amino acid sequence and peptide conformation. The juxtaposition of a hydrophilic residue with a hydrophobic aromatic moiety provides a simplified system for analyzing intramolecular interactions, hydrogen bonding, and backbone flexibility. Such studies contribute to a deeper understanding of how dipeptide composition influences secondary structure formation and stability, which is essential for rational peptide design and protein engineering.
Enzymatic substrate specificity: The dipeptide serves as a reference substrate in enzymology, particularly for investigating the activity and selectivity of peptidases and proteases. By monitoring the hydrolysis of Thr-Phe, researchers can assess enzyme preferences for specific sequence motifs, cleavage patterns, and catalytic efficiency. Insights gained from these assays inform the development of enzyme inhibitors, the characterization of proteolytic pathways, and the optimization of industrial biocatalytic processes.
Peptide transport and absorption studies: Thr-Phe is employed in transport assays to probe the mechanisms of dipeptide uptake across biological membranes, such as those mediated by peptide transporters in cellular or intestinal systems. Its defined structure and detectability make it an ideal candidate for tracing absorption kinetics, transporter affinity, and competitive inhibition. These studies are instrumental in advancing knowledge of nutrient assimilation, drug delivery strategies, and the functional characterization of membrane proteins involved in peptide translocation.
Analytical method development: The dipeptide is widely used as a calibration standard and reference compound in chromatographic and mass spectrometric analyses of peptides. Its physicochemical properties, including solubility and ionization behavior, facilitate method optimization for peptide detection, quantitation, and separation. Employing Thr-Phe as a benchmark compound ensures reliable analytical performance in quality control, metabolomics, and proteomics workflows.
Peptide synthesis optimization: Researchers leverage Thr-Phe to evaluate and refine synthetic protocols in solid-phase and solution-phase peptide synthesis. Its straightforward sequence enables precise monitoring of coupling efficiency, deprotection steps, and purification procedures. By systematically studying the synthesis of this dipeptide, chemists can identify and mitigate challenges related to peptide bond formation, side reactions, and product isolation, ultimately improving yield and reproducibility in the generation of more complex peptides.
2. Implications of ligand-receptor binding kinetics on GLP-1R signalling
4. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
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