H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH includes aromatic, polar, acidic, and basic residues that generate a multifaceted folding landscape. Researchers explore its structural behavior through hydrogen-bond mapping and conformational analysis. The peptide supports studies of binding-site architecture. Applications include sequence optimization, structural modeling, and biophysical research.
CAT No: R2472
CAS No:960358-79-6
Synonyms/Alias:H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH;960358-79-6;
H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH is a synthetic peptide sequence engineered for advanced research applications in biochemistry, molecular biology, and biomedical sciences. Featuring a unique arrangement of amino acids, this peptide offers a versatile platform for investigating protein-protein interactions, signaling pathways, and structure-function relationships in peptide science. Its well-defined primary structure allows for precise experimental manipulation, making it a valuable tool for elucidating complex biological mechanisms. The presence of both hydrophilic and hydrophobic residues supports its integration into various assay systems, while the multiple lysine and glutamic acid units provide potential sites for conjugation, labeling, or further chemical modification. As a research-grade peptide, it is widely recognized for its stability and compatibility with a range of in vitro experimental protocols.
Peptide-Protein Interaction Studies: H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH serves as an important probe in the study of peptide-protein interactions, enabling researchers to dissect binding affinities and specificities within complex biological contexts. By incorporating this peptide into binding assays, scientists can map interaction domains, evaluate the effects of amino acid substitutions, and identify novel binding partners. Such studies are crucial for understanding the molecular underpinnings of cellular processes and for the rational design of peptide-based modulators. The sequence's diversity of charged and polar residues facilitates its use in pull-down assays and co-immunoprecipitation experiments, further expanding its utility in proteomic research.
Signal Transduction Pathway Analysis: In the field of cell signaling, this synthetic peptide is frequently employed to investigate the modulation of intracellular pathways. Its sequence can mimic or competitively inhibit endogenous peptides, thereby allowing researchers to probe the roles of specific signaling cascades. By introducing the peptide into cultured cells or biochemical systems, investigators can monitor downstream effects such as phosphorylation events, second messenger production, or gene expression changes. These insights are invaluable for unraveling the complexities of cellular communication and for identifying potential targets for therapeutic intervention.
Enzyme Substrate Characterization: The sequence H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH is also utilized as a substrate in enzymatic assays, particularly for proteases and peptidases. Its defined structure allows for precise monitoring of cleavage events, enabling the characterization of enzyme specificity, kinetics, and inhibition. By tracking the generation of peptide fragments, researchers can elucidate mechanisms of enzyme action, screen for inhibitors, and develop new assay formats. This application is especially relevant in drug discovery and in the study of post-translational modifications.
Peptide-Based Structural Studies: Structural biologists leverage this peptide for elucidating secondary and tertiary structure formation using techniques such as NMR spectroscopy, circular dichroism, and X-ray crystallography. Its balanced composition of alpha-helix and beta-sheet-promoting residues provides a model system for studying folding dynamics, stability, and conformational changes. Insights gained from these studies contribute to a deeper understanding of the principles governing protein architecture and inform the design of novel biomolecules with tailored properties.
Antibody Production and Epitope Mapping: Due to its well-defined and immunogenic sequence, the peptide is frequently used as an antigen for generating specific antibodies in research animals. These antibodies are subsequently applied in Western blotting, ELISA, and immunoprecipitation assays to detect and quantify target proteins. Additionally, the peptide facilitates epitope mapping studies, enabling the identification of antibody binding sites and the optimization of immunoassay sensitivity and specificity. Such applications are integral to the advancement of diagnostic and analytical methodologies in life sciences.
Bioconjugation and Functionalization Studies: Researchers often employ H-Phe-Asn-Pro-Ser-Gly-Pro-Tyr-Gln-Lys-Lys-Pro-Val-His-Glu-Lys-Lys-Glu-Val-Leu-OH as a scaffold for bioconjugation, attaching fluorescent dyes, affinity tags, or other functional groups to its lysine and glutamic acid residues. This enables the development of labeled probes for imaging, tracking, or quantification in a variety of biological systems. The peptide's adaptability to chemical modification supports the creation of multifunctional constructs for targeted delivery, biosensing, or surface immobilization. Through these diverse applications, this synthetic peptide continues to play a pivotal role in advancing fundamental and applied research across molecular and cellular biology.
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