H-Tyr-Cys(1)-Asp-Glu-His-Phe-Cys(1)-Tyr-OH forms a compact peptide with two cysteines capable of generating a stabilizing disulfide bond. Aromatic and charged residues create a balanced folding environment. Researchers study pH-dependent dynamics and binding tendencies. Applications include motif-function exploration, oxidative folding research, and peptide engineering.
CAT No: R2564
CAS No:629628-53-1
Synonyms/Alias:Kp7-6;629628-53-1;HY-P10102;DA-54658;CS-0906978;
H-Tyr-Cys(1)-Asp-Glu-His-Phe-Cys(1)-Tyr-OH is a synthetic peptide featuring a specific sequence of amino acids, including tyrosine, cysteine, aspartic acid, glutamic acid, histidine, and phenylalanine. As a custom-designed peptide, it provides a valuable tool for researchers investigating peptide structure-function relationships, protein interactions, and the role of disulfide bonds in biochemical systems. Its sequence, which includes two cysteine residues capable of forming intramolecular or intermolecular disulfide bridges, makes it particularly relevant for studies focused on peptide folding, stability, and conformational analysis. The presence of both acidic and aromatic residues further enhances its utility in exploring diverse biochemical phenomena, ranging from molecular recognition to binding affinity assessments.
Peptide structure-function analysis: Researchers frequently employ this synthetic peptide to elucidate the relationship between amino acid sequence and biological activity. By systematically modifying or analyzing the sequence, scientists can gain insights into how specific residues or motifs contribute to overall peptide conformation, stability, and function. The inclusion of cysteine residues is especially significant, as it allows for the study of disulfide bond formation and its impact on tertiary structure, which is crucial for understanding the folding and stability of larger proteins and peptide-based biomolecules.
Protein-protein interaction studies: The defined sequence and chemical properties of this peptide make it a useful probe for investigating molecular interactions with proteins, receptors, or other biomolecules. By serving as a ligand or binding partner in affinity assays, it enables the characterization of binding kinetics, specificity, and affinity. Such studies are fundamental for mapping interaction domains, identifying critical contact points, and developing peptide-based inhibitors or modulators for biochemical research.
Peptide synthesis validation: In the context of solid-phase peptide synthesis and analytical method development, this peptide serves as a valuable reference or standard. Its sequence complexity, including the presence of aromatic, acidic, and sulfur-containing residues, challenges synthetic protocols and purification strategies. Successful synthesis and characterization of this peptide help validate synthetic methodologies, optimize purification workflows, and assess the performance of analytical techniques such as HPLC or mass spectrometry.
Conformational and stability studies: The sequence's propensity to form disulfide bonds and adopt defined secondary structures makes it an ideal candidate for studies focused on peptide folding, conformational dynamics, and stability under varying environmental conditions. Researchers can use it to systematically evaluate the influence of pH, temperature, or redox state on peptide conformation and to investigate mechanisms of disulfide exchange or isomerization. Such experiments contribute to a deeper understanding of peptide resilience and folding pathways relevant to both basic and applied biochemical sciences.
Biochemical assay development: The unique sequence and functional groups present in this peptide facilitate its use in the design and optimization of biochemical assays. Whether employed as a substrate, probe, or calibrant, it enables the development of sensitive and specific assays for enzyme activity, binding studies, or detection of redox changes. Its versatility supports a wide range of experimental formats, from spectroscopic and chromatographic analyses to high-throughput screening platforms, thereby enhancing the reliability and reproducibility of peptide-based research methodologies.
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