Dansyl-Gly-Cys-Val-Leu-Ser-OH contains a dansyl fluorophore attached to a pentapeptide featuring a reactive cysteine. Hydrophobic residues support membrane or protein-surface association, while the fluorophore enables environment-sensitive detection. Researchers use it to monitor thiol reactivity, binding events, and microenvironment polarity. Applications include fluorescence labeling, probe development, and peptide-protein interaction studies.
CAT No: R2592
CAS No:143744-88-1
Synonyms/Alias:Dansyl-Gly-Cys-Val-Leu-Ser-OH;143744-88-1;Dansyl-GCVLS;Dansyl-Gly-Cys-Val-Leu-Ser;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[2-[[5-(Dimethylamino)naphthalen-1-yl]sulfonylamino]acetyl]amino]-3-sulfanylpropanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoic acid;MFCD04974167;SCHEMBL9073673;CHEMBL2314094;HY-P4337;DA-62661;FD110983;CS-0653684;
Dansyl-Gly-Cys-Val-Leu-Ser-OH is a synthetic peptide featuring an N-terminal dansyl (5-dimethylaminonaphthalene-1-sulfonyl) group, which imparts distinct fluorescence properties to the molecule. As a pentapeptide composed of glycine, cysteine, valine, leucine, and serine, it serves as a versatile tool in biochemical and molecular biology research. The inclusion of the dansyl moiety enables sensitive detection and quantification in a variety of analytical and functional assays, making the compound particularly valuable in studies that require precise monitoring of peptide interactions, enzymatic processing, or cellular uptake. Its defined sequence and functional groups allow for targeted investigation of structure-activity relationships, peptide transport mechanisms, and protein-peptide interactions.
Fluorescence-based detection: The dansyl label on this peptide provides strong fluorescence emission, enabling its use as a probe in fluorescence spectroscopy, HPLC, and capillary electrophoresis. Researchers utilize the compound to track peptide dynamics, monitor enzymatic degradation, or quantify peptide concentrations in complex biological samples. Its high sensitivity and compatibility with standard fluorescence instrumentation make it an excellent choice for real-time or end-point detection in biochemical assays.
Enzyme substrate studies: The sequence and structure of Dansyl-Gly-Cys-Val-Leu-Ser-OH make it suitable as a model substrate for protease and peptidase activity assays. By monitoring changes in fluorescence as the peptide is cleaved, investigators can characterize enzyme specificity, kinetics, and inhibition profiles. This approach streamlines the development of enzyme inhibitors and supports mechanistic studies of proteolytic pathways relevant to cellular regulation and signal transduction.
Peptide transport and cellular uptake assays: The fluorescent properties of the dansyl group facilitate the investigation of peptide transport mechanisms across biological membranes. The compound is frequently employed to study uptake kinetics, subcellular localization, and transporter specificity in cell-based models. Its defined structure allows for the systematic evaluation of sequence-dependent transport phenomena, contributing to a deeper understanding of peptide delivery and cellular import processes.
Protein-peptide interaction analysis: The labeled peptide serves as a functional probe for exploring protein-peptide interactions, including binding affinity, specificity, and conformational changes. Fluorescence-based binding assays using this compound enable quantitative and qualitative assessment of molecular recognition events, supporting the identification of peptide ligands, mapping of protein interaction sites, and elucidation of binding mechanisms in signaling or regulatory networks.
Peptide structure-activity relationship (SAR) studies: The defined sequence and functional labeling of Dansyl-Gly-Cys-Val-Leu-Ser-OH support its use in SAR investigations, where modifications to amino acid composition or labeling are systematically assessed for their impact on biological activity or binding properties. Such studies provide critical insights into the determinants of peptide function, inform rational design of bioactive peptides, and advance the development of novel research tools in molecular pharmacology and chemical biology.
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