H-His-Ala-Ile-Tyr-Pro-Arg-His-OH combines aromatic, hydrophobic, and basic residues arranged to form stable, compact motifs. Histidines provide pH-sensitive coordination sites, while proline imposes local conformational constraints. Researchers explore hydrogen-bonding and folding in solution. Applications include peptide-protein interaction studies, motif mapping, and conformational analysis.
CAT No: R2381
CAS No:268215-17-4
Synonyms/Alias:CHEMBL3265326;268215-17-4;HAIYPRH hydrochloride?;DTXSID60436301;BDBM50015534;
H-His-Ala-Ile-Tyr-Pro-Arg-His-OH is a synthetic peptide composed of seven amino acid residues arranged in a precise sequence. As a heptapeptide, it features a combination of histidine, alanine, isoleucine, tyrosine, proline, and arginine residues, each contributing distinct physicochemical and functional properties. The specific arrangement of these amino acids imparts unique structural motifs and potential for biological activity, making this peptide a valuable tool for biochemical research. Its design allows for targeted investigation into peptide structure-function relationships, receptor interactions, and enzymatic processing, which are central themes in peptide science and molecular biology.
Peptide structure-activity relationship studies: Researchers frequently employ this heptapeptide in systematic investigations aimed at elucidating how sequence variations influence biological activity. By analyzing the impact of each amino acid within the sequence, scientists can gain insight into the structural determinants that govern peptide-receptor binding, conformational stability, and molecular recognition. Such studies are fundamental to the rational design of bioactive peptides and the development of peptide-based probes or modulators.
Enzymatic substrate analysis: The sequence of H-His-Ala-Ile-Tyr-Pro-Arg-His-OH offers a defined substrate for characterizing the specificity and kinetics of various proteases and peptidases. By monitoring the cleavage patterns and enzymatic processing of this peptide, researchers can profile enzyme activity, identify cleavage sites, and assess inhibitor potency in vitro. These analyses are critical for understanding proteolytic pathways and for developing selective enzyme inhibitors or activity-based assays.
Receptor binding and signaling research: Due to the presence of residues commonly found in endogenous signaling peptides, this heptapeptide is frequently utilized in studies exploring peptide-receptor interactions. Its sequence enables the examination of binding affinities, receptor selectivity, and downstream signaling events using biochemical and cell-based assays. Such applications support the discovery of novel ligand-receptor pairs and enhance understanding of peptide-mediated signaling mechanisms.
Analytical method development: The defined composition and sequence of this peptide make it a suitable standard or model for developing and validating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its use in method development allows for the optimization of peptide separation, detection, and quantitation, supporting the advancement of analytical workflows in proteomics and quality control laboratories.
Peptide synthesis optimization: As a representative sequence with diverse side-chain functionalities, H-His-Ala-Ile-Tyr-Pro-Arg-His-OH serves as a practical model for evaluating and refining solid-phase peptide synthesis protocols. Researchers can use it to assess coupling efficiency, deprotection strategies, and purification procedures, thereby improving synthetic yields and product purity. Insights gained from such optimization efforts contribute to the broader field of peptide chemistry and facilitate the production of complex peptide analogs for research applications.
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