Thr-Val is a dipeptide linking polar threonine with hydrophobic valine, serving as a model for β-branched interactions. Researchers investigate its hydrogen-bonding behavior and solvent-dependent conformations. Applications include folding studies, enzyme-substrate modeling, and dipeptide-based design.
CAT No: R2382
CAS No:99032-17-4
Synonyms/Alias:H-Thr-Val-OH;threonyl-valine;99032-17-4;Thr-Val;Threonylvaline;L-threonyl-L-valine;Threoninylvaline;TV dipeptide;T-V Dipeptide;L-Threoninyl-L-Valine;Threonine Valine dipeptide;Threonine-Valine dipeptide;CHEBI:90328;(2S)-2-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]-3-methylbutanoic acid;(S)-2-((2S,3R)-2-Amino-3-hydroxybutanamido)-3-methylbutanoic acid;N-Threonylvaline;N-Threoninylvaline;L-Thr-L-Val;N-L-Threonyl-L-valine;N-L-Threoninyl-L-valine;FT108190;Q27162466;
Thr-Val, also known as Threonylvaline, is a dipeptide composed of threonine and valine linked by a peptide bond. With its unique combination of hydrophilic and hydrophobic amino acid residues, Thr-Val exhibits distinctive physicochemical properties that make it valuable for a range of biochemical and research-oriented applications. The presence of threonine introduces a hydroxyl group, enhancing solubility and reactivity, while valine contributes structural stability and hydrophobic interactions. This dipeptide serves as a convenient model for studying peptide bond formation, enzymatic hydrolysis, and peptide transport mechanisms. Researchers in peptide chemistry, molecular biology, and analytical science utilize Thr-Val as a versatile tool for investigating fundamental processes and developing novel methodologies.
Peptide Transport Studies: Thr-Val is frequently employed in investigations of peptide transport across biological membranes. As a small, well-characterized dipeptide, it serves as an ideal substrate for probing the specificity and kinetics of peptide transporters such as those in the SLC15 family. By tracking the uptake and efflux of Thr-Val in cellular models, researchers can elucidate transporter mechanisms, identify potential inhibitors, and explore the physiological relevance of dipeptide transport in nutrient absorption and drug delivery systems.
Enzymatic Hydrolysis Research: Threonylvaline is widely used as a substrate to study the activity and specificity of peptidases and proteases. Its defined structure allows for precise monitoring of enzymatic cleavage events, providing insights into enzyme-substrate interactions and catalytic mechanisms. By utilizing this dipeptide in hydrolysis assays, scientists can characterize new enzymes, screen for inhibitory compounds, and optimize reaction conditions for industrial or laboratory-scale peptide processing.
Peptide Bond Formation Mechanisms: The synthesis and analysis of Thr-Val offer a model system for examining peptide bond formation, both in solution and on solid-phase supports. Researchers leverage its manageable size and defined sequence to optimize coupling reagents, assess racemization, and develop new synthetic protocols. Studies involving this dipeptide contribute to advancements in peptide synthesis methodology, facilitating the efficient generation of longer and more complex peptides for research and development purposes.
Analytical Method Development: Threonylvaline serves as a standard or calibrant in the development of analytical techniques such as high-performance liquid chromatography (HPLC), capillary electrophoresis, and mass spectrometry. Its physicochemical properties and well-characterized behavior make it suitable for method validation, instrument calibration, and the establishment of reference retention times or fragmentation patterns. Analytical chemists rely on this dipeptide to ensure reproducibility and accuracy in the quantification and identification of peptides in complex mixtures.
Structure-Activity Relationship (SAR) Studies: The use of Thr-Val in SAR investigations enables researchers to probe the influence of dipeptide composition on biological activity, stability, and interaction with biomolecules. By comparing the properties of threonylvaline with other dipeptides, scientists can identify key structural features that govern recognition by enzymes, receptors, or transporters. These studies inform the rational design of bioactive peptides, peptidomimetics, and peptide-based materials for diverse scientific and technological applications.
In summary, Threonylvaline stands out as a valuable dipeptide for research in peptide transport, enzymatic hydrolysis, synthetic methodology, analytical technique development, and structure-activity relationship analysis. Its well-defined structure, balanced chemical characteristics, and compatibility with a wide array of experimental systems make it an indispensable tool in the exploration of peptide science and the advancement of related disciplines.
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