Sar-Arg-Val-Tyr-Ile-His-Pro-Phe begins with sarcosine, introducing N-methylation that affects backbone flexibility and enzyme recognition. The remaining residues provide a balance of hydrophobic, aromatic, and basic functionalities. Researchers employ the sequence to model receptor-binding epitopes and peptide-protein contacts. Applications include ligand-optimization projects, signaling-pathway analysis, and structure-activity investigations.
CAT No: R2709
CAS No:102029-89-0
Synonyms/Alias:Sar-Arg-Val-Tyr-Ile-His-Pro-Phe;102029-89-0;N-Methylglycyl-N~5~-(diaminomethylidene)ornithylvalyltyrosylisoleucylhistidylprolylphenylalanine--acetic acid (1/1);acetic acid;2-[[1-[2-[[2-[[2-[[2-[[5-(diaminomethylideneamino)-2-[[2-(methylamino)acetyl]amino]pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoic acid;VIPLPZKDKSDVMT-UHFFFAOYSA-N;PAN-3948-PI;DTXSID50657523;H-Sar-Arg-Val-Tyr-Ile-His-Pro-Phe-OH;
Sar-Arg-Val-Tyr-Ile-His-Pro-Phe is a synthetic peptide composed of eight amino acid residues, engineered to serve as a valuable tool in peptide research and biochemical investigations. Its sequence, featuring both natural and modified amino acids, allows for the exploration of structure-activity relationships and receptor interactions within various biological systems. As a research-use peptide, it offers a versatile platform for probing protein-peptide interactions, signal transduction mechanisms, and the design of novel biomolecular tools. The unique arrangement of residues, including a sarcosine (N-methylglycine) at the N-terminus, enhances its stability and can modulate its biological properties, making it an important resource for advanced peptide-based studies.
Receptor binding studies: Researchers frequently employ this octapeptide in the analysis of receptor-ligand interactions, particularly within the context of G protein-coupled receptors or other peptide-responsive cellular targets. Its defined sequence enables systematic investigation of binding affinity, specificity, and downstream signaling events, facilitating the elucidation of molecular recognition processes. The presence of both hydrophobic and basic residues within the peptide chain further supports its utility in dissecting the contributions of individual side chains to receptor engagement.
Peptide structure-activity relationship (SAR) analysis: The sequence serves as a model system for SAR studies, where modifications at specific positions can reveal critical determinants of biological activity. By substituting, truncating, or modifying individual residues, scientists can map functional hotspots and optimize peptide analogs for enhanced stability, potency, or selectivity. Such investigations are fundamental to the rational design of peptide-based probes, inhibitors, or mimetics in both academic and industrial settings.
Enzymatic stability and protease profiling: The inclusion of a sarcosine residue at the N-terminus renders the peptide resistant to certain exopeptidases, making it particularly useful in enzymatic degradation assays. Researchers use it to assess the substrate specificity of proteases, evaluate enzyme kinetics, and develop strategies for improving peptide stability in biological environments. This application is especially relevant in the context of drug discovery, where metabolic stability is a key consideration for peptide therapeutics and diagnostics.
Peptide synthesis optimization: The defined sequence and moderate length of this octapeptide make it an ideal reference compound for evaluating solid-phase peptide synthesis (SPPS) methodologies. Laboratories utilize it to benchmark coupling efficiencies, test novel protecting group strategies, and validate purification protocols. The presence of challenging residues such as arginine and histidine provides a rigorous test for synthesis and purification workflows, supporting the advancement of peptide chemistry techniques.
Biochemical assay development: The peptide is also employed as a substrate, standard, or control in a variety of biochemical assays. Its well-characterized sequence and predictable physicochemical properties facilitate its use in binding assays, enzyme activity measurements, and signal transduction studies. By serving as a reliable reference molecule, it enables the calibration and validation of experimental protocols across diverse research applications, contributing to reproducibility and data quality in peptide-focused investigations.
1. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
2. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
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