Cyclo(-Pro-Thr) is a diketopiperazine formed by cyclization of proline and threonine, generating a rigid heterocycle with defined stereochemistry. The structure encourages β-turn mimicry and reduces backbone flexibility. Researchers use it to explore conformational constraints, peptide stabilization, and ligand-design principles. Its compact ring system supports detailed structural and mechanistic studies.
CAT No: R2280
CAS No:227777-31-3
Synonyms/Alias:Cyclo(-Pro-Thr);227777-31-3;Cyclo(Pro-Thr);(3S,8aS)-3-[(1R)-1-hydroxyethyl]-2,3,6,7,8,8a-hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;(3S,8aS)-Hexahydro-3-[(1R)-1-hydroxyethyl]pyrrolo[1,2-a]pyrazine-1,4-dione;MFCD05663455;HY-P5050;(3S,8aS)-3-((R)-1-hydroxyethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;AKOS006293957;DA-62585;FC108331;CS-0675916;
Cyclo(-Pro-Thr), also known as cyclo(Prolyl-Threonyl), is a cyclic dipeptide belonging to the diketopiperazine family, a class of naturally occurring and synthetic compounds with notable biochemical and structural properties. As a conformationally constrained molecule formed by the cyclization of proline and threonine residues, it exhibits enhanced stability and resistance to proteolytic degradation compared to linear peptides. The unique ring structure of this diketopiperazine imparts distinct physicochemical characteristics, making it a valuable scaffold for research into peptide conformation, molecular recognition, and structure-activity relationships. Its presence in various natural sources and its synthetic accessibility have drawn significant interest in the fields of chemical biology, peptide chemistry, and biomolecular engineering.
Peptide conformation studies: Cyclo(-Pro-Thr) serves as a model compound for investigating the conformational behavior of cyclic dipeptides. Its rigid backbone and defined stereochemistry provide an excellent system for elucidating the influence of ring formation on peptide secondary structure and intramolecular interactions. Researchers utilize this diketopiperazine to gain insights into the conformational preferences of cyclic peptides, which is critical for the rational design of bioactive molecules and the development of peptide-based therapeutics.
Peptide synthesis research: The compound is frequently employed as a reference standard or intermediate in peptide synthesis workflows. Its well-characterized structure and stability make it a useful benchmark for optimizing cyclization reactions, evaluating synthetic methodologies, and validating analytical techniques such as HPLC, NMR, and mass spectrometry. Additionally, it aids in the development of novel synthetic strategies for generating structurally diverse diketopiperazines and related macrocyclic peptides.
Molecular recognition and binding studies: Due to its constrained cyclic structure, cyclo(Prolyl-Threonyl) is utilized in studies exploring molecular recognition processes, particularly those involving protein-ligand or peptide-receptor interactions. The diketopiperazine ring serves as a privileged scaffold in the design of molecular probes and mimetics, enabling researchers to dissect the determinants of binding affinity, specificity, and selectivity in diverse biological systems. Its use in these studies contributes to a deeper understanding of the principles governing biomolecular interactions.
Chemical biology tool development: The structural features of cyclo(-Pro-Thr) make it an attractive building block for the development of chemical biology tools and functionalized probes. By leveraging its cyclic nature and modifiable side chains, scientists can derivatize the molecule to create fluorescent tags, affinity labels, or crosslinking agents tailored for target identification, protein labeling, or interaction mapping in complex biological environments. Such applications expand the utility of diketopiperazines in probing cellular processes and elucidating molecular mechanisms.
Analytical method validation: The compound's defined composition and stability render it a valuable standard for validating and calibrating analytical techniques used in peptide research. Laboratories often employ cyclo(Prolyl-Threonyl) as a control in chromatographic and spectrometric analyses to ensure method accuracy, reproducibility, and sensitivity. Its consistent behavior under various analytical conditions supports quality assurance in peptide characterization and quantification workflows, facilitating reliable experimental outcomes.
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