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 is a synthetic dipeptide composed of aspartic acid and valine, representing a fundamental building block in peptide chemistry and protein research. As a member of the peptide compound category, it embodies both acidic and branched-chain amino acid residues, offering a unique combination of physicochemical properties. Its sequence is commonly encountered in protein structures and bioactive peptide motifs, making it a valuable model for investigating peptide behavior, structure-activity relationships, and enzymatic processing. The precise arrangement of an acidic side chain and a hydrophobic branched side chain in Asp-Val contributes to its utility in a wide array of biochemical and analytical contexts, supporting research into peptide function, synthesis, and interaction dynamics.
Peptide synthesis research: Asp-Val serves as a reliable model dipeptide for optimizing solid-phase peptide synthesis protocols and evaluating coupling reagents. Its sequence is often used to assess the efficiency of peptide bond formation, particularly between residues with differing side chain characteristics. By incorporating this dipeptide into synthetic workflows, researchers can systematically study factors such as racemization, side chain protection strategies, and the influence of sequence context on yield and purity, thereby refining methodologies for more complex peptide targets.
Protease substrate studies: The dipeptide is frequently employed as a reference substrate for examining the specificity and catalytic mechanisms of proteolytic enzymes, including exopeptidases and endopeptidases. The presence of both aspartic acid and valine offers an informative substrate for mapping enzyme cleavage preferences, facilitating the development of enzyme assays and inhibitor screening platforms. Insights gained from such studies are instrumental in elucidating protease function and guiding the design of selective modulators.
Peptide structure-function analysis: As a representative short peptide, Asp-Val is utilized in biophysical investigations aimed at understanding peptide folding, conformational dynamics, and intermolecular interactions. Its combination of polar and hydrophobic residues provides a simplified model for exploring secondary structure formation and aggregation tendencies. These studies contribute to broader knowledge regarding the determinants of peptide stability and activity, informing the rational design of functional peptides and peptide-based materials.
Analytical method development: The dipeptide is valuable in the calibration and validation of chromatographic and mass spectrometric techniques for peptide analysis. Its defined sequence and predictable retention behavior make it an ideal standard for method optimization, including the assessment of resolution, sensitivity, and reproducibility in peptide quantification workflows. Utilizing Asp-Val as a reference compound enhances the reliability of analytical platforms employed in proteomics, quality control, and bioanalytical research.
Peptide-based material science: The unique physicochemical properties of Asp-Val have prompted its use in the development and characterization of peptide-based hydrogels, nanomaterials, and surface coatings. Researchers exploit its dual nature—combining anionic and hydrophobic elements—to tailor material properties such as self-assembly, solubility, and interfacial behavior. Such applications are relevant to the design of biomimetic materials, drug delivery vehicles, and biosensor interfaces, where precise control over peptide interactions and material architecture is required.
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