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 the amino acids threonine and valine linked via a peptide bond. As a member of the peptide compound category, Thr-Val serves as a valuable biochemical tool in peptide research, offering insight into peptide structure, function, and interaction dynamics. Its unique sequence allows researchers to probe the roles of specific dipeptide motifs in biological systems, making it relevant in studies that explore protein folding, enzyme specificity, and molecular recognition. The compound's physicochemical properties and defined composition further support its use in various experimental and analytical contexts within the broader field of life sciences.
Peptide synthesis research: Thr-Val is frequently utilized as a model substrate in peptide synthesis studies. Its defined sequence and manageable size make it an ideal candidate for optimizing solid-phase peptide synthesis protocols and assessing coupling efficiency. Researchers often employ this dipeptide to evaluate the performance of different coupling reagents, resin types, and deprotection strategies, which are critical for developing robust and scalable synthetic methodologies. Insights gained from such experiments contribute to the refinement of synthetic techniques for larger, more complex peptides and proteins.
Protease substrate studies: As a well-characterized dipeptide, Thr-Val is valuable for investigating the substrate specificity and catalytic mechanisms of various proteolytic enzymes. By incorporating it into enzymatic assays, scientists can determine the cleavage preferences of serine proteases, metalloproteases, and other peptidases. These studies are essential for elucidating enzyme function, mapping active sites, and developing selective inhibitors or activity-based probes. The use of dipeptides like Thr-Val in such assays provides precise control over substrate structure, enabling detailed kinetic and mechanistic analyses.
Peptide transport and uptake research: The dipeptide is also employed in studies focused on peptide transporters and membrane uptake mechanisms. By tracking the cellular or vesicular uptake of Thr-Val, researchers can characterize the specificity and transport kinetics of oligopeptide transport systems such as PEPT1 and PEPT2. These investigations inform our understanding of nutrient absorption, drug delivery strategies, and the physiological regulation of peptide transport across biological membranes. The use of structurally defined dipeptides is crucial for dissecting the molecular determinants that govern transporter-substrate interactions.
Analytical method development: Thr-Val serves as a reference standard and calibration compound in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-defined molecular weight and chemical properties make it suitable for optimizing separation parameters, assessing instrument sensitivity, and establishing quantification protocols for peptide analysis. Reliable analytical methods are essential for quality control, peptide quantitation, and the characterization of complex biological samples.
Functional peptide studies: The dipeptide is further used in research exploring the structure-activity relationships of bioactive peptides. By incorporating Thr-Val into peptide libraries or synthetic analogs, scientists can investigate how specific dipeptide motifs influence biological function, receptor binding, or signaling pathway modulation. Such studies advance the rational design of peptides with tailored properties for use in biochemical assays, material science, or as molecular probes in fundamental research. The ability to systematically vary sequence elements using simple dipeptides like Thr-Val provides a foundation for decoding the functional logic of peptide-based systems.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More