Iyptngytr is a nonapeptide containing aromatic, polar, and charged residues that encourage β-turn formation and solvent-sensitive folding. Researchers use it to investigate ligand-recognition motifs, hydrogen-bonding patterns, and conformational transitions. The sequence's varied polarity supports modeling of protein-peptide interfaces. Its compact length enables focused structural analysis.
CAT No: R2270
CAS No:1431957-72-0
Synonyms/Alias:IYPTNGYTR;1431957-72-0;HY-P3147;AKOS040756799;CS-0149484;(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[2-[[(2S)-4-amino-2-[[(2S,3R)-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxybutanoyl]amino]-4-oxobutanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid;
Iyptngytr is a synthetic peptide compound designed for advanced biochemical and molecular research applications. Composed of a specific sequence of amino acids, it demonstrates unique structural and functional properties that make it a valuable tool in peptide-focused studies. The sequence and configuration of Iyptngytr allow for targeted investigation of peptide interactions, receptor binding, and structure-activity relationships, supporting a broad range of research initiatives in the life sciences. Its defined molecular architecture provides a reliable platform for studies requiring precise control over peptide composition and behavior.
Peptide-receptor interaction studies: As a custom peptide, Iyptngytr is frequently utilized to probe the specificity and affinity of peptide-receptor interactions. Researchers employ it in binding assays to elucidate the molecular mechanisms underlying signal transduction or ligand recognition by cellular receptors. The defined sequence allows for systematic evaluation of key residues involved in binding, facilitating the mapping of interaction sites and the identification of critical determinants of biological activity.
Structure-activity relationship (SAR) analysis: The compound serves as an essential model in the assessment of how amino acid sequence variations influence peptide function. By systematically modifying or comparing Iyptngytr with related peptides, scientists can dissect the contributions of individual residues to overall activity, stability, or conformational preferences. Such SAR studies are instrumental in guiding the rational design of new peptide analogs with enhanced or tailored properties for research and development purposes.
Peptide synthesis validation: Iyptngytr is often used as a reference or test substrate in the optimization and validation of solid-phase peptide synthesis protocols. Its defined sequence and physicochemical characteristics make it suitable for evaluating coupling efficiency, protecting group strategies, and purification methods. Successful synthesis and characterization of this peptide can serve as a benchmark for troubleshooting and refining peptide manufacturing workflows in research settings.
Analytical method development: The peptide's distinct sequence and properties render it a valuable standard for developing and calibrating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Laboratories employ Iyptngytr to assess method sensitivity, resolution, and reproducibility, ensuring robust detection and quantification of peptide analytes in complex mixtures. This supports quality control and method validation processes across various research applications.
Biochemical assay development: Iyptngytr is incorporated into the design and optimization of in vitro biochemical assays aimed at studying enzymatic activity, substrate specificity, or peptide modification processes. Its well-characterized nature allows for controlled experimentation, enabling researchers to monitor reaction kinetics, product formation, or post-translational modifications with high precision. This utility extends to the development of novel assay formats and the standardization of experimental protocols in peptide biochemistry.
1. TMEM16F and dynamins control expansive plasma membrane reservoirs
2. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
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