H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH arranges acidic, basic, aromatic, and hydrophobic residues to create a versatile model for folding studies. The peptide supports examination of hydrogen bonding, charge distribution, and side-chain packing. Researchers assess its binding properties across varied environments. Applications include motif exploration, biophysical studies, and synthetic peptide design.
CAT No: R2440
CAS No:812644-79-4
Synonyms/Alias:TRV056;812644-79-4;HY-P3137;AKOS040758362;DA-68379;CS-0148149;G18155;
H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH, also known as a nonapeptide with a defined amino acid sequence, is a synthetic peptide widely utilized in biochemical research for its unique structural and functional properties. Comprising nine amino acids, this peptide sequence offers a versatile model for studying peptide-protein interactions, receptor binding, and signal transduction mechanisms. Its precise arrangement of hydrophilic and hydrophobic residues allows for the investigation of conformational dynamics and structure-activity relationships, making it a valuable tool for elucidating the molecular underpinnings of biological processes. The presence of both charged and aromatic side chains within the sequence further enhances its utility in mimicking biologically relevant motifs, thereby facilitating a range of experimental applications.
Receptor-Ligand Interaction Studies: H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH is frequently employed in studies exploring the specificity and affinity of peptide-receptor binding. By serving as a ligand in in vitro assays, researchers can investigate how structural modifications affect binding kinetics and downstream signaling events. The peptide's sequence, rich in both basic and aromatic residues, makes it particularly suitable for mapping interaction sites on G protein-coupled receptors and other membrane-bound proteins, providing insights into the molecular determinants of receptor activation and inhibition.
Signal Transduction Pathway Analysis: Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH is also instrumental in dissecting intracellular signaling cascades. Its ability to mimic endogenous peptide motifs enables researchers to study phosphorylation events, second messenger generation, and protein-protein interactions within various cellular contexts. By introducing this nonapeptide into cell-based assays, scientists can monitor alterations in kinase activity or transcription factor localization, thereby advancing the understanding of complex signaling networks.
Enzyme Substrate Characterization: The peptide sequence serves as a substrate for various proteolytic enzymes, such as serine or metalloproteases, in enzymology research. By analyzing the cleavage patterns and kinetics of enzymatic reactions involving H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH, researchers can elucidate substrate specificity, catalytic efficiency, and the influence of sequence context on enzyme activity. This information is crucial for the rational design of enzyme inhibitors or modulators in biochemical studies.
Peptide Structure-Function Relationship Studies: Nonapeptides like Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH are valuable for probing the relationship between primary sequence, secondary structure, and biological function. Utilizing techniques such as circular dichroism spectroscopy, NMR, or X-ray crystallography, scientists can assess how specific amino acid substitutions or modifications influence peptide folding, stability, and bioactivity. These studies inform the rational engineering of peptides with enhanced properties for research applications.
Drug Discovery and Screening Platforms: In pharmaceutical research, H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH is incorporated into high-throughput screening assays to identify novel modulators of protein-protein interactions or enzyme activity. Its defined sequence provides a consistent and reproducible scaffold for assessing the efficacy of small molecules, peptides, or biologics in modulating target pathways. By integrating this peptide into assay platforms, researchers can accelerate the identification of lead compounds and optimize hit-to-lead processes.
Biomaterials and Surface Modification: The nonapeptide's amphipathic nature and sequence diversity make it suitable for applications in biomaterials engineering and surface functionalization. By attaching Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH to polymeric or inorganic surfaces, researchers can modulate cellular adhesion, proliferation, or differentiation in tissue engineering constructs. Its ability to present specific recognition motifs enables the design of bioactive surfaces that direct cell behavior or mediate selective biomolecular interactions, thereby expanding its utility in regenerative medicine and biosensor development. Through these diverse application areas, H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH continues to play a pivotal role in advancing scientific research and innovation across multiple disciplines.
2. High fat diet and GLP-1 drugs induce pancreatic injury in mice
3. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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