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, also known as a heptapeptide composed of histidine, alanine, isoleucine, tyrosine, proline, arginine, and histidine residues, is a synthetic peptide with unique structural and biochemical properties. This compound is characterized by its specific amino acid sequence, which imparts distinct conformational features and potential for diverse interactions with biological targets. The presence of both aromatic and basic residues within its sequence allows for potential binding capabilities, making it a valuable molecular tool in various research and development settings. Its solubility profile and stability under standard laboratory conditions further support its utility in experimental protocols that require reliable and reproducible peptide reagents.
Peptide-based receptor studies: H-His-Ala-Ile-Tyr-Pro-Arg-His-OH is frequently employed in investigations targeting peptide-receptor interactions. Researchers utilize this heptapeptide to probe the binding affinities and specificity of receptors, particularly those implicated in signal transduction pathways. By introducing the peptide into in vitro systems, scientists can monitor receptor activation, downstream signaling events, and competitive binding dynamics, thereby elucidating the molecular mechanisms underlying receptor function. Such studies are essential for understanding cellular communication and for identifying potential modulators of receptor activity.
Enzyme substrate analysis: The sequence of this heptapeptide renders it a suitable substrate or reference compound for enzyme activity assays, especially those involving proteolytic enzymes. Enzymologists can incorporate the peptide into their assays to evaluate enzymatic cleavage patterns, substrate specificity, and reaction kinetics. The resulting data help to map enzyme active sites and contribute to the rational design of enzyme inhibitors or modified substrates. Utilizing this peptide as a model substrate streamlines the process of characterizing novel enzymes and optimizing reaction conditions in biochemical research.
Cellular uptake and transport research: H-His-Ala-Ile-Tyr-Pro-Arg-His-OH serves as a model compound in studies focused on cellular uptake, peptide transport mechanisms, and intracellular trafficking. Its defined sequence allows for the tracking of peptide movement across cellular membranes and the assessment of uptake efficiency under various experimental conditions. By conjugating the peptide with fluorescent tags or isotopic labels, researchers can visualize and quantify its distribution within cells, thereby advancing the understanding of peptide transporters and endocytic pathways.
Structure-activity relationship (SAR) exploration: This heptapeptide is utilized in structure-activity relationship studies to determine how specific amino acid substitutions impact biological activity. Scientists systematically modify individual residues within the sequence to generate peptide analogs and then assess changes in binding affinity, stability, or functional outcomes. These SAR investigations provide invaluable insights into the critical determinants of peptide function and inform the rational design of novel peptides with enhanced properties for research or industrial applications.
Biomarker discovery and assay development: H-His-Ala-Ile-Tyr-Pro-Arg-His-OH is integrated into proteomic workflows aimed at identifying peptide-based biomarkers or developing analytical assays. Its well-defined structure makes it an ideal standard or reference material for method calibration, quantification, and validation in mass spectrometry or immunoassay platforms. By leveraging this peptide, researchers can improve assay sensitivity, reproducibility, and specificity, thereby facilitating the detection and quantification of target peptides in complex biological samples.
Peptide library construction: In the context of combinatorial chemistry and high-throughput screening, this heptapeptide is incorporated into peptide libraries to expand the diversity of screened compounds. Its sequence serves as a scaffold for generating variant peptides, enabling the identification of candidates with desirable binding or functional characteristics. Through iterative synthesis and screening, scientists can discover novel ligands, enzyme substrates, or molecular probes that advance the frontiers of peptide-based research and development. The versatility of H-His-Ala-Ile-Tyr-Pro-Arg-His-OH thus positions it as a foundational tool in peptide science, supporting innovation across multiple disciplines.
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