Cyclo(Ile-Ala) is a diketopiperazine combining isoleucine and alanine to form a rigid ring that mimics β-turn geometries. The structure provides steric constraints that influence aggregation behavior and solvent interactions. Researchers use it to model constrained backbones and peptide stability. Its compactness allows straightforward biophysical evaluation.
CAT No: R2285
CAS No:90821-99-1
Synonyms/Alias:Cyclo(Ile-Ala);90821-99-1;3-butan-2-yl-6-methylpiperazine-2,5-dione;SCHEMBL17867288;DTXSID801334341;HY-N9251;KBA59069;KBA59070;AKOS012403656;DA-62581;MS-22991;CS-0159114;3-(2-Butanyl)-6-methyl-2,5-piperazinedione;G14094;3-METHYL-6-(SEC-BUTYL)PIPERAZINE-2,5-DIONE;
Cyclo(Ile-Ala) is a cyclic dipeptide composed of isoleucine and alanine residues linked via a peptide bond to form a stable diketopiperazine ring structure. As a member of the diketopiperazine family, this compound exhibits notable conformational rigidity and resistance to enzymatic degradation, making it a valuable scaffold in biochemical and pharmaceutical research. Its unique cyclic structure imparts distinct physicochemical properties, including enhanced stability and potential for specific molecular interactions, which are of interest in the study of peptide conformation, molecular recognition, and bioactive compound development. Cyclo(Ile-Ala) serves as a versatile tool for researchers investigating peptide-based mechanisms, structure-activity relationships, and applications in diverse biochemical contexts.
Peptide Conformation Studies: Due to its cyclic nature, Cyclo(Ile-Ala) is frequently utilized in research focused on peptide folding, rigidity, and conformational analysis. The diketopiperazine core provides a model system for understanding how cyclization influences the three-dimensional structure of peptides, which is crucial for elucidating the determinants of molecular stability and biological function. Its well-defined structure allows for detailed spectroscopic and crystallographic investigations, offering insights into intramolecular hydrogen bonding, ring strain, and conformational preferences that inform the design of novel cyclic peptides.
Template for Peptide Synthesis: The compound's robust diketopiperazine scaffold is valued as a synthetic intermediate and template in the generation of more complex peptide architectures. Researchers employ Cyclo(Ile-Ala) as a building block in solid-phase and solution-phase peptide synthesis to introduce conformational constraints or to serve as a precursor for structurally diverse peptide derivatives. Its use facilitates the creation of libraries of cyclic and linear peptides with tailored properties, supporting the exploration of structure-activity relationships and the development of peptide-based probes or ligands.
Molecular Recognition and Binding Studies: The stability and defined geometry of Cyclo(Ile-Ala) make it an effective probe for investigating molecular recognition processes, including protein-peptide and peptide-receptor interactions. Its cyclic structure enables the study of binding specificity, affinity, and selectivity in biochemical systems, providing a controlled platform for dissecting non-covalent interactions such as hydrogen bonding, hydrophobic contacts, and van der Waals forces. These studies are instrumental in advancing the understanding of molecular recognition mechanisms relevant to drug discovery and biomolecular engineering.
Analytical Reference Standard: In analytical chemistry, Cyclo(Ile-Ala) is employed as a reference standard for the identification and quantification of diketopiperazines in complex biological or environmental samples. Its well-characterized physicochemical properties, including chromatographic behavior and spectroscopic signatures, facilitate method development and validation in techniques such as HPLC, mass spectrometry, and NMR spectroscopy. Using this compound as a standard supports accurate profiling of cyclic dipeptides, which is valuable for quality control, metabolomics, and food chemistry research.
Chemical Biology Probing: The compound's resistance to enzymatic hydrolysis and structural similarity to bioactive peptides render it a useful probe in chemical biology studies. Cyclo(Ile-Ala) can be applied to investigate peptide transport, metabolism, and stability in cellular or enzymatic systems, providing insights into the fate and function of cyclic peptides in biological environments. These applications contribute to a deeper understanding of peptide-based signaling, transport mechanisms, and the metabolic pathways involved in peptide turnover, enhancing knowledge relevant to both fundamental and applied biochemical research.
1. The spatiotemporal control of signalling and trafficking of the GLP-1R
2. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
3. Emu oil in combination with other active ingredients for treating skin imperfections
5. Cationic cell-penetrating peptides are potent furin inhibitors
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More