Val-Ser pairs hydrophobic valine with polar serine to investigate hydrogen-bond formation and side-chain interactions. The dipeptide adopts conformations that help model early folding events. Researchers explore its behavior in solvent-accessibility and enzymatic recognition studies. Use includes peptide-synthesis development, structural motif research, and interaction mapping.
CAT No: R2631
CAS No:13588-94-8
Synonyms/Alias:H-Val-Ser-OH;13588-94-8;L-valyl-L-serine;val-ser;Valylserine;(S)-2-((S)-2-Amino-3-methylbutanamido)-3-hydroxypropanoic acid;valyl-serine;VS dipeptide;V-S Dipeptide;CHEBI:75021;Valine Serine dipeptide;Valine-Serine dipeptide;L-Val-L-Ser;(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-hydroxypropanoic acid;NSC 339921;N-Valylserine;(2S)-2-(((2S)-2-amino-3-methylbutanoyl)amino)-3-hydroxypropanoic acid;(2S)-2-(((2S)-2-azaniumyl-3-methylbutanoyl)amino)-3-hydroxypropanoate;(2S)-2-[[(2S)-2-azaniumyl-3-methylbutanoyl]amino]-3-hydroxypropanoate;MFCD00056712;Val-L-Ser, L-;CHEMBL1221610;VS;AKOS010408211;CS-W010491;HY-W009775;FV108233;Q27145080;(S)-2-((S)-2-Amino-3-methylbutanamido)-3-hydroxypropanoicacid;(2S)-2-[(2S)-2-AMINO-3-METHYLBUTANAMIDO]-3-HYDROXYPROPANOIC ACID;
Val-Ser, also known as Valylserine, is a dipeptide composed of the amino acids valine and serine linked via a peptide bond. As a member of the peptide compound category, Val-Ser exhibits unique biochemical characteristics that make it a valuable tool in research focused on peptide structure, function, and bioactivity. Its sequence, which combines a hydrophobic branched-chain residue (valine) with a polar hydroxyl-containing residue (serine), provides a model system for investigating intermolecular interactions, peptide conformational dynamics, and enzymatic processing. The versatility of Val-Ser as a minimalistic peptide motif allows for its integration into a variety of experimental designs within biochemistry, molecular biology, and peptide-based technology development.
Peptide synthesis research: Val-Ser is frequently utilized as a building block in solid-phase peptide synthesis (SPPS) and solution-phase strategies. Its dipeptide format enables researchers to study coupling efficiency, protecting group strategies, and optimization of peptide elongation protocols. By incorporating Val-Ser into synthetic schemes, chemists can investigate the influence of sequence order and side-chain functionality on reaction kinetics and product yields, thereby refining methodologies for the assembly of more complex peptide sequences.
Enzyme substrate specificity studies: As a defined dipeptide, Val-Ser serves as a model substrate for characterizing the activity and specificity of proteases, peptidases, and other peptide-modifying enzymes. Researchers employ it to elucidate cleavage preferences, mechanistic pathways, and kinetic parameters, particularly for enzymes that recognize or process short peptide motifs. The differential properties of valine and serine side chains provide insight into substrate recognition and catalytic efficiency, supporting the rational design of enzyme inhibitors or activity assays.
Peptide transport and uptake investigations: The dipeptide is valuable in studies of peptide transporters, such as those in bacterial, mammalian, or plant systems. Its physicochemical properties—arising from the combination of hydrophobic and polar residues—make it a suitable probe for examining the selectivity, kinetics, and regulatory mechanisms of oligopeptide transport proteins. By tracking the cellular or vesicular uptake of Val-Ser, researchers can dissect the molecular determinants of transporter-mediated peptide absorption and distribution.
Structure-function relationship analysis: Val-Ser provides a simplified model for exploring how short peptide sequences influence secondary structure formation, intermolecular interactions, and functional properties. Its dual-residue composition allows for systematic investigation of hydrogen bonding, hydrophobic packing, and the role of side-chain chemistry in modulating peptide conformation. These studies contribute to a broader understanding of the principles governing protein folding, aggregation, and biomolecular recognition.
Analytical method development: The defined nature and stability of Val-Ser make it a convenient standard or reference compound in the development and validation of analytical techniques, such as high-performance liquid chromatography (HPLC), mass spectrometry (MS), and capillary electrophoresis (CE). It is used to calibrate instruments, optimize separation conditions, and evaluate detection limits for peptide analysis. The presence of both hydrophobic and polar functional groups in Val-Ser aids in assessing chromatographic behavior and ionization efficiency, supporting robust analytical workflows in peptide research and quality control.
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