H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH forms a long peptide rich in acidic, basic, aromatic, and hydrophobic regions. The complex residue distribution generates a multidomain folding landscape. Researchers investigate hydrogen bonding, intramolecular interactions, and solvent-dependent structure. Applications include structural biophysics, peptide engineering, and motif-based studies.
CAT No: R2680
CAS No:186359-67-1
Synonyms/Alias:H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH;186359-67-1;H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH;CID 131636539;
H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH, a synthetic peptide with a defined amino acid sequence, offers a unique platform for scientific research and advanced biochemical investigations. Characterized by its sequence of hydrophilic and hydrophobic residues, this peptide is advantageous for studies requiring a stable, customizable biomolecule. Its structure enables interactions with various biological targets, opening avenues for applications in molecular recognition, protein-protein interaction analysis, and as a model system for peptide folding and dynamics. The presence of charged and aromatic side chains within the sequence further enhances its utility in binding studies, facilitating research into the mechanisms of molecular affinity and specificity. Researchers value this peptide for its consistency, reliability, and versatility in experimental design, making it a valuable tool across multiple domains of life sciences.
Protein-Protein Interaction Studies: H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH serves as an effective probe for elucidating the intricacies of protein-protein interactions. Its carefully designed sequence allows it to mimic or disrupt natural binding motifs, enabling researchers to dissect the molecular determinants of complex formation. By incorporating this peptide into binding assays, scientists can map interaction sites, investigate affinity changes due to sequence modifications, and gain insights into the structural basis of protein assembly. Such studies are critical for understanding cellular signaling pathways and the molecular underpinnings of disease.
Enzyme Substrate and Inhibitor Research: The peptide's diverse amino acid composition makes it an excellent candidate for enzyme substrate or inhibitor studies. Enzymologists can employ it to determine substrate specificity, measure catalytic activity, or screen for enzyme inhibitors. By monitoring the peptide's cleavage or modification in the presence of specific enzymes, researchers can characterize enzyme kinetics and develop novel modulators for biochemical pathways. This approach is particularly valuable in the study of proteases, kinases, and other peptide-modifying enzymes, facilitating the discovery of new regulatory mechanisms.
Structural Biology and Folding Analysis: As a model system, this peptide is instrumental in exploring the principles of peptide folding and conformational stability. Its sequence, which includes both helix- and sheet-promoting residues, allows structural biologists to investigate secondary structure formation using spectroscopic and computational techniques. The peptide's response to environmental changes, such as pH or solvent conditions, provides valuable data on folding dynamics and aggregation tendencies. These insights contribute to a deeper understanding of protein misfolding diseases and the development of peptide-based therapeutics.
Binding Affinity and Biosensor Development: The sequence of H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH is well-suited for integration into biosensor platforms. Its capacity to interact with target molecules, such as antibodies, receptors, or small ligands, makes it a valuable recognition element in diagnostic assays. By immobilizing the peptide on sensor surfaces, researchers can develop highly sensitive and specific detection systems for a range of analytes. These biosensors are instrumental in advancing point-of-care diagnostics, environmental monitoring, and food safety testing.
Peptide-Based Material Science: Beyond traditional biochemical applications, this peptide finds utility in the development of advanced biomaterials. Its amphiphilic nature and sequence-driven self-assembly properties enable the creation of nanostructures, hydrogels, or surface coatings with tailored functionalities. Material scientists exploit the peptide's ability to form ordered assemblies, incorporating it into scaffolds for tissue engineering, drug delivery systems, or as templates for inorganic material synthesis. Such innovations underscore the peptide's versatility and its role in bridging the gap between biology and materials science.
In summary, H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-OH offers a multifaceted platform for scientific exploration. Its applications span protein interaction analysis, enzymology, structural biology, biosensor development, and material science, providing researchers with a robust and adaptable tool for advancing knowledge in both fundamental and applied research contexts.
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