Asp-Val pairs a strongly acidic residue with a hydrophobic valine, offering insight into charge-hydrophobic interplay during early folding events. Researchers examine its hydrogen-bond potential and solvent behavior. The dipeptide aids studies of enzymatic specificity and protonation effects. Applications span structural modeling, peptide design, and biochemical mechanism studies.
CAT No: R2665
CAS No:13433-04-0
Synonyms/Alias:H-Asp-Val-OH;Asp-Val;13433-04-0;Aspartyl-Valine;l-aspartyl-l-valine;CHEMBL441685;CHEBI:73832;(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-3-methylbutanoic acid;L-Asp-L-Val;alpha-aspartylvaline;MFCD00037285;L-alpha-Asp-L-Val;L-alpha-aspartyl-L-valine;L-I+/--Aspartyl-L-valine;SCHEMBL3785072;(S)-3-Amino-4-(((S)-1-carboxy-2-methylpropyl)amino)-4-oxobutanoic acid;DTXSID001314995;HY-P4313;BDBM50188511;DA-74019;FA108008;CS-0653482;Q27144150;(2S)-2-[(2S)-2-AMINO-3-CARBOXYPROPANAMIDO]-3-METHYLBUTANOIC ACID;(S)-3-amino-4-((S)-1-carboxy-2-methylpropylamino)-4-oxobutanoic acid;
Asp-Val, also known as Aspartylvaline, is a dipeptide composed of the amino acids aspartic acid and valine linked by a peptide bond. This compound stands out for its unique structural properties, which make it a valuable tool in biochemical and molecular research. Its stable peptide linkage and defined sequence allow for precise applications in studies involving peptide function, enzymatic activity, and protein engineering. Researchers frequently utilize Asp-Val as a model dipeptide to explore the fundamental principles of peptide chemistry and to investigate the interactions between amino acid residues in short peptide chains. Its solubility and compatibility with a variety of analytical techniques further enhance its utility across multiple scientific disciplines.
Peptide Structure Analysis: Asp-Val is widely used in peptide structure analysis to investigate the conformational preferences and interactions between amino acid side chains. By incorporating this dipeptide into experimental systems, scientists can study the impact of aspartic acid's carboxyl group and valine's hydrophobic side chain on overall peptide structure. This information is crucial for understanding the folding and stability of larger proteins, as well as for designing synthetic peptides with tailored properties. The insights gained from these studies contribute to the broader field of protein engineering and help inform the development of novel biomolecules.
Enzymatic Substrate Studies: In enzymology, Asp-Val acts as a model substrate for the investigation of protease specificity and catalytic mechanisms. Researchers employ this dipeptide to assess the substrate preferences of various proteolytic enzymes, including those involved in cellular regulation and signal transduction. By analyzing the rates and patterns of Asp-Val hydrolysis, scientists can elucidate enzyme-substrate interactions and identify key determinants of enzyme activity. These findings have implications for the design of enzyme inhibitors and the development of new biochemical assays.
Peptide Transport Mechanism Research: Aspartylvaline is instrumental in exploring peptide transport mechanisms across biological membranes. Its relatively simple structure makes it an ideal candidate for studying the uptake and translocation of dipeptides by peptide transporters, such as those found in cellular membranes. By tracking the movement of Asp-Val in model systems, researchers can gain insights into the selectivity, kinetics, and regulation of peptide transporters, which are essential for nutrient absorption and cellular homeostasis. This knowledge supports the advancement of research in membrane biology and pharmacokinetics.
Peptidomimetic Design and Synthesis: The dipeptide Asp-Val serves as a foundational building block in the design and synthesis of peptidomimetics—compounds that mimic the structure and function of natural peptides. By incorporating this motif into larger molecules, chemists can create analogs with enhanced stability, bioavailability, or target specificity. The use of Asp-Val in peptidomimetic research enables the development of innovative molecules for applications in biotechnology, diagnostics, and molecular recognition.
Biochemical Assay Development: Researchers frequently incorporate Aspartylvaline into biochemical assays as a standard or control peptide. Its defined sequence and predictable behavior make it well-suited for calibrating analytical instruments, validating assay protocols, and benchmarking experimental results. The use of Asp-Val in assay development ensures reproducibility and accuracy in peptide quantification, enzyme kinetics studies, and high-throughput screening applications. As a result, it plays an important role in supporting robust scientific research and facilitating the discovery of new biomolecular interactions.
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