Hexa-Cys-Pro-Pro-Thr-Gln-Phe-Cys-COOH contains multiple cysteines, enabling rich disulfide chemistry and metal-binding exploration. Proline residues impose local turns, while phenylalanine contributes hydrophobic stabilization. Researchers examine its folding pathways and oxidative transitions. Applications include redox-active peptide research, metallopeptide studies, and disulfide-topology mapping.
CAT No: R2590
CAS No:2581199-34-8
Synonyms/Alias:2581199-34-8;EX-A7826F;Hexa-Cys-Pro-Pro-Thr-Gln-Phe-Cys-COOH;Hexanoyl-L-cysteinyl-L-prolyl-L-prolyl-L-threonyl-L-glutaminyl-L-phenylalanyl-L-cysteine;
Hexa-Cys-Pro-Pro-Thr-Gln-Phe-Cys-COOH is a synthetic peptide featuring a defined amino acid sequence capped with a carboxyl group at the C-terminus. As a custom-designed peptide, it incorporates multiple cysteine residues, which are often leveraged for their potential to form disulfide bonds and facilitate structural motifs relevant to protein folding and stability. The inclusion of proline, threonine, glutamine, and phenylalanine provides additional structural diversity, influencing the peptide's conformational properties and functional capabilities. Such peptides serve as valuable molecular tools in biochemical research, enabling targeted investigation of sequence-specific interactions, structure-function relationships, and peptide-based engineering strategies.
Peptide structure-function studies: The sequence of Hexa-Cys-Pro-Pro-Thr-Gln-Phe-Cys-COOH is particularly well-suited for probing the relationship between primary structure and higher-order conformation in peptides. The presence of multiple cysteine residues enables the formation of intra- or intermolecular disulfide bridges, which are crucial for stabilizing secondary and tertiary structures. Researchers employ such peptides in biophysical assays, including circular dichroism and NMR spectroscopy, to investigate folding pathways, conformational stability, and the impact of specific residue arrangements on overall peptide architecture.
Disulfide bond engineering: Due to its cysteine-rich composition, this peptide is frequently utilized in studies focused on disulfide bond formation and isomerization. It serves as a model substrate in enzymatic assays involving protein disulfide isomerase or other thiol-disulfide oxidoreductases. By monitoring the kinetics and specificity of disulfide bond formation, scientists can gain insights into oxidative protein folding mechanisms, redox regulation, and the development of novel strategies for stabilizing synthetic peptides or engineered proteins.
Peptide-protein interaction assays: The defined sequence of Hexa-Cys-Pro-Pro-Thr-Gln-Phe-Cys-COOH allows it to function as a probe in binding studies with target proteins or receptors. Its unique motif can be exploited in affinity chromatography, surface plasmon resonance, or fluorescence polarization assays to characterize sequence-dependent binding affinities, map interaction domains, and elucidate the molecular determinants of peptide recognition. These applications are critical for advancing understanding of protein-ligand interactions and for the rational design of peptide-based affinity reagents.
Peptide synthesis and analytical method development: As a representative example of a cysteine-containing peptide, this compound is valuable in optimizing solid-phase peptide synthesis protocols, particularly those involving the selective protection and deprotection of thiol groups. Analytical laboratories utilize it as a reference standard to validate chromatographic or mass spectrometric methods for peptide characterization, including assessment of purity, identity, and correct disulfide connectivity. Such methodological advancements are essential for ensuring the quality and reproducibility of peptide-based products in research and industry.
Biomaterials and surface modification: The multiple cysteine residues present in the peptide sequence facilitate covalent attachment to gold surfaces or other thiol-reactive substrates, making it a practical choice for surface functionalization studies. Researchers employ this peptide to create bioactive coatings, immobilize biomolecules, or engineer peptide-based nanostructures for biosensing, diagnostics, or materials science applications. The ability to control peptide orientation and density on surfaces enables the development of advanced platforms for molecular recognition and signal transduction studies.
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