MM 419447 contains a structured peptide-like backbone suitable for modeling molecular recognition and conformational adaptability. Residue variability supports investigations of hydrophobic-polar balance. Researchers utilize it to examine ligand binding and steric complementarity. Use cases include peptide mimic design, structure-activity exploration, and receptor-mapping studies.
CAT No: R2296
CAS No:1092457-78-7
Synonyms/Alias:MM 419447;1092457-78-7;SCHEMBL24483647;AKOS040756463;DA-75639;(1R,4S,7S,13S,16R,21R,24R,27S,30S,33R,38R,44S)-21-amino-13-(2-amino-2-oxoethyl)-27-(2-carboxyethyl)-44-[(1R)-1-hydroxyethyl]-30-[(4-hydroxyphenyl)methyl]-4-methyl-3,6,12,15,22,25,28,31,40,43,46,51-dodecaoxo-18,19,35,36,48,49-hexathia-2,5,11,14,23,26,29,32,39,42,45,52-dodecazatetracyclo[22.22.4.216,33.07,11]dopentacontane-38-carboxylic acid;
MM 419447 is a synthetic peptide compound designed for advanced biochemical research applications. As a structurally defined peptide, it offers precise sequence fidelity, enabling researchers to probe specific molecular interactions and signaling pathways with high specificity. The compound's unique primary structure makes it a valuable tool for investigating protein-protein interactions, receptor binding events, and post-translational modification dynamics. Its stability and compatibility with a range of in vitro systems further enhance its utility in both fundamental and applied peptide science, where reproducibility and molecular definition are critical.
Peptide-Protein Interaction Studies: MM 419447 is highly suitable for elucidating the molecular basis of peptide-mediated protein interactions. By serving as a defined ligand or substrate in binding assays, it enables researchers to dissect the affinities and kinetics of interactions involving target proteins, receptors, or enzymes. This capability is essential for mapping interaction domains, characterizing binding motifs, and understanding the mechanistic underpinnings of signal transduction cascades in cellular systems.
Receptor Binding Assays: The compound's well-characterized sequence and chemical stability make it an ideal probe in receptor binding studies. It can be employed to assess the specificity and strength of peptide-receptor interactions, facilitating the identification of critical residues involved in ligand recognition. Such assays are fundamental in exploring receptor activation, downstream signaling events, and the competitive binding of endogenous or synthetic analogs, thereby supporting the rational design of new modulators or inhibitors.
Peptide Structure-Function Analysis: MM 419447 provides a robust platform for structure-function investigations, where systematic modifications to its sequence can reveal the relationship between peptide conformation and biological activity. Researchers can utilize the peptide in mutagenesis or truncation studies to pinpoint essential amino acids and structural motifs responsible for functional outcomes. These analyses are instrumental in advancing the understanding of bioactive peptide mechanisms and in guiding the engineering of optimized analogs for research purposes.
Analytical Method Development: The defined nature of MM 419447 makes it an excellent reference standard or calibration tool in analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its predictable chromatographic and spectrometric behavior allows for the validation of peptide detection methods, quantification protocols, and purity assessments. This application supports laboratories in achieving accurate, reproducible analytical results when working with complex peptide mixtures or during method validation processes.
Peptide Synthesis and Modification Research: The compound serves as a model substrate for exploring novel strategies in peptide synthesis and post-synthetic modifications. Its compatibility with various chemical and enzymatic modification protocols enables the development and optimization of labeling, cyclization, or conjugation techniques. By providing a consistent and well-characterized template, MM 419447 aids researchers in refining synthetic methodologies and expanding the toolkit for custom peptide engineering in biochemical studies.
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