H-Cys(1)-Ser-Cys(2)-Ser-Ser-Leu-Met-Asp-Lys-Glu-Cys(2)-Val-Tyr-Phe-Cys(1)-His-Leu-Asp-Ile-Ile-Trp-Val-Asn-Thr-Pro-Glu-His-Val-Val-Pro-Tyr-OH features multiple cysteine residues forming potential disulfide networks that stabilize complex tertiary structures. The diverse residue distribution shapes hydrophobic, polar, and charged regions within the peptide. Researchers analyze its conformational behavior and binding interactions across varied environments. Applications include structural biology, sequence engineering, and motif-based functional studies.
CAT No: R2427
CAS No:133972-52-8
Synonyms/Alias:H-Cys(1)-Ser-Cys(2)-Ser-Ser-Leu-Met-Asp-Lys-Glu-Cys(2)-Val-Tyr-Phe-Cys(1)-His-Leu-Asp-Ile-Ile-Trp-Val-Asn-Thr-Pro-Glu-His-Val-Val-Pro-Tyr-OH;133972-52-8;
H-Cys(1)-Ser-Cys(2)-Ser-Ser-Leu-Met-Asp-Lys-Glu-Cys(2)-Val-Tyr-Phe-Cys(1)-His-Leu-Asp-Ile-Ile-Trp-Val-Asn-Thr-Pro-Glu-His-Val-Val-Pro-Tyr-OH is a custom-designed peptide sequence recognized for its intricate arrangement of amino acids and the presence of multiple cysteine residues, which can facilitate the formation of disulfide bonds. This peptide's unique primary structure enables it to adopt stable secondary and tertiary conformations, making it a valuable tool in various biochemical and molecular biology research applications. Its sequence complexity, including hydrophilic and hydrophobic residues, allows for versatile interactions with proteins, nucleic acids, and other biomolecules, supporting advanced studies in protein engineering, structural biology, and signal transduction. The presence of functional groups such as thiol, amide, and carboxyl moieties further enhances its reactivity and utility in conjugation chemistry, labeling studies, and as a scaffold for molecular recognition.
Protein-Protein Interaction Studies: H-Cys(1)-Ser-Cys(2)-Ser-Ser-Leu-Met-Asp-Lys-Glu-Cys(2)-Val-Tyr-Phe-Cys(1)-His-Leu-Asp-Ile-Ile-Trp-Val-Asn-Thr-Pro-Glu-His-Val-Val-Pro-Tyr-OH is frequently employed in research focused on elucidating protein-protein interactions, especially where disulfide bond formation plays a critical role in stabilizing complexes. The peptide's multiple cysteine residues can form intramolecular or intermolecular disulfide linkages, enabling researchers to mimic or disrupt natural protein conformations and study the effects on binding affinity, specificity, and downstream signaling pathways. By introducing this peptide into in vitro assays or cellular systems, scientists can probe the mechanisms of redox-dependent interactions and map contact sites within multi-protein assemblies.
Structural Biology and Folding Studies: The sequence's capacity for adopting defined secondary structures makes it an excellent model for investigating protein folding, misfolding, and aggregation phenomena. Researchers utilize this peptide to study the thermodynamics and kinetics of folding transitions, leveraging spectroscopic techniques such as circular dichroism or NMR to monitor conformational changes. The presence of aromatic and hydrophobic residues further allows for the exploration of core packing and surface exposure, providing insights into the principles governing protein stability and the formation of functional domains.
Enzyme Substrate and Inhibitor Design: As a synthetic substrate or competitive inhibitor, this peptide is invaluable for characterizing enzyme specificity, catalytic efficiency, and active site architecture. Its diverse amino acid composition and modifiable termini enable precise tailoring for use in protease assays, kinase substrate profiling, or as a scaffold for peptidomimetic inhibitor development. By systematically modifying residues within the sequence, researchers can dissect structure-activity relationships and optimize lead compounds for further study.
Affinity Purification and Biomolecular Labeling: The functional groups present within the peptide, notably the thiol side chains of cysteine residues, facilitate site-specific conjugation to affinity tags, fluorescent dyes, or biotin moieties. This capability allows for the creation of highly selective probes for affinity purification of interacting proteins or nucleic acids from complex biological samples. Additionally, labeled derivatives of the peptide can be used in imaging, localization, or tracking studies, enhancing the resolution and sensitivity of detection in both in vitro and in vivo experiments.
Biomaterials and Nanotechnology: The robust secondary structure and chemical reactivity of this peptide sequence make it an attractive building block for the design of novel biomaterials and nanostructures. By exploiting disulfide-mediated crosslinking, researchers can fabricate self-assembling hydrogels, nanofibers, or surface coatings with tunable mechanical and biochemical properties. These peptide-based materials find application in biosensing, drug delivery, and tissue engineering, where precise control over molecular architecture and functionalization is essential for performance and biocompatibility.
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