AC1Olrh5 is a synthetic small molecule containing aromatic and heterocyclic domains designed to modulate noncovalent interactions. Researchers examine its conformational flexibility, electronic distribution, and binding potential. Its scaffold supports mechanistic mapping and structure-function correlation. The molecule's versatility aids chemical biology investigations.
CAT No: R2286
CAS No:16691-00-2
Synonyms/Alias:CYCLO(-GLU-GLU);16691-00-2;AC1OLRH5;3-[(2S,5S)-5-(2-carboxyethyl)-3,6-dioxopiperazin-2-yl]propanoic acid;DTXSID50428619;2,5-Piperazinedipropanoic acid, 3,6-dioxo-, (2S,5S)-;MFCD00237611;DTXCID30379453;HY-P4615;AS-85914;DA-72464;FC108011;CS-0655408;G15666;3,3'-((2S,5S)-3,6-Dioxopiperazine-2,5-diyl)dipropionic acid;
AC1Olrh5 is a synthetic peptide compound designed for advanced research in the fields of biochemistry, molecular biology, and peptide engineering. As a structurally defined peptide, it offers a valuable tool for probing protein-protein interactions, elucidating signaling pathways, and supporting the development of novel biomolecular assays. Its sequence and conformational properties make it particularly suitable for studies requiring precise modulation of biological processes or the creation of peptide-based analytical platforms. The compound's chemical stability and ease of incorporation into experimental systems further enhance its utility across a range of technical applications.
Peptide interaction studies: AC1Olrh5 can be employed as a model ligand or binding partner in the investigation of protein-peptide and peptide-peptide interactions. Its defined sequence enables researchers to dissect the molecular determinants of binding specificity and affinity, supporting the mapping of interaction interfaces in complex biological systems. Such studies are critical for understanding signaling cascades, regulatory mechanisms, and the structural basis of macromolecular assembly.
Peptide synthesis validation: The compound serves as a benchmark or reference standard in the optimization and validation of solid-phase peptide synthesis protocols. Its well-characterized structure allows laboratories to assess the efficiency of coupling reactions, monitor side-product formation, and refine purification strategies. By providing a reliable synthetic target, it facilitates the troubleshooting and improvement of peptide production workflows, contributing to higher yields and enhanced product quality in research and development settings.
Functional assay development: AC1Olrh5 is frequently utilized in the design and calibration of functional assays that rely on peptide substrates or modulators. Its biochemical properties make it suitable for use in enzyme activity assays, receptor binding studies, or high-throughput screening platforms. By serving as a consistent and reproducible component, it enables the generation of robust assay data and supports the evaluation of novel compounds or biological targets.
Structural biology research: The defined nature of this peptide makes it an ideal candidate for structural studies using techniques such as NMR spectroscopy, circular dichroism, or crystallography. Incorporating AC1Olrh5 into experimental systems allows researchers to investigate peptide folding, conformational dynamics, and secondary structure formation. Insights gained from these studies contribute to a deeper understanding of peptide stability, aggregation tendencies, and the relationship between sequence and structural properties.
Peptide modification and conjugation studies: Researchers often utilize AC1Olrh5 as a substrate for chemical modification, conjugation, or labeling experiments. Its sequence can be selectively derivatized with functional groups, fluorescent tags, or affinity handles, enabling the exploration of site-specific modifications and their impact on peptide behavior. These applications are essential for the development of targeted delivery systems, imaging probes, and multifunctional biomolecules in both fundamental and applied research contexts.
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