Cyclo(-Met-Pro) forms a diketopiperazine ring linking methionine and proline in a compact, conformationally restricted scaffold. The thioether side chain offers a handle for redox chemistry and metal-binding studies. Researchers investigate its backbone geometry, hydrogen bonding, and pH-dependent behavior. Applications include cyclic-dipeptide modeling, natural-product mimicry, and stability profiling.
CAT No: R2571
CAS No:53049-06-2
Synonyms/Alias:Cyclo(-Met-Pro);cyclo(methionylpropyl);53049-06-2;(3S,8aS)-3-(2-methylsulfanylethyl)-2,3,6,7,8,8a-hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;MFCD03093468;CHEMBL463747;SCHEMBL16853544;DTXSID601346730;HMS1702I07;HY-P1937;STL565779;AKOS000739486;FC108324;CS-0100109;BRD-K00331588-001-01-2;(3S,8AS)-3-(2-(methylthio)ethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;(3S,8aS)-3-[2-(methylsulfanyl)ethyl]hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;
Cyclo(-Met-Pro) is a cyclic dipeptide, also known as a diketopiperazine, composed of methionine and proline residues linked in a head-to-tail fashion. As a member of the diketopiperazine family, it exhibits notable chemical stability and conformational rigidity, making it of considerable interest in peptide chemistry and natural product research. Its occurrence in various biological systems, coupled with its unique structural attributes, has positioned this compound as a valuable model for investigating peptide cyclization, conformational analysis, and structure-activity relationships. Researchers utilize Cyclo(-Met-Pro) to explore the fundamental properties of cyclic peptides as well as their broader implications in biochemical and biophysical studies.
Peptide structure-function analysis: Cyclo(-Met-Pro) serves as a reference compound for elucidating the impact of cyclization on peptide backbone conformation and stability. Its rigid cyclic structure offers an ideal platform for examining how peptide ring closure influences resistance to enzymatic degradation and affects overall molecular dynamics. By comparing the properties of this diketopiperazine to its linear counterparts, researchers gain important insights into the relationship between peptide architecture and biological function, supporting the rational design of more stable peptide-based molecules.
Natural product mimicry and biosynthetic studies: The compound is frequently employed as a model system for studying diketopiperazine biosynthesis and occurrence in nature. Its structural motif is commonly found in microbial metabolites and secondary metabolites of higher organisms, making it a useful probe for investigating biosynthetic pathways, enzymatic cyclization mechanisms, and the functional roles of cyclic dipeptides in ecological and physiological contexts. Such studies contribute to a deeper understanding of natural product diversity and the enzymology underlying peptide cyclization.
Analytical method development: Cyclo(-Met-Pro) is utilized as a standard or calibration compound in the development and validation of chromatographic and spectrometric techniques for peptide analysis. Its well-defined structure and distinct physicochemical properties enable precise method optimization for the detection, separation, and quantification of small cyclic peptides. Analytical chemists leverage these attributes to refine protocols for quality control, purity assessment, and structural elucidation of related compounds in research and industrial settings.
Peptide synthesis and chemical modification: The compound acts as a valuable building block and intermediate in synthetic peptide chemistry. Its cyclic scaffold is exploited in the design and synthesis of novel peptide derivatives, peptidomimetics, and hybrid molecules with tailored biological and physicochemical properties. Researchers use Cyclo(-Met-Pro) to investigate strategies for cyclization, backbone modification, and functional group diversification, supporting the development of new molecules for biochemical assays, material science applications, and fundamental research.
Conformational and biophysical studies: The diketopiperazine framework of Cyclo(-Met-Pro) provides a model system for probing peptide folding, intramolecular interactions, and solvent effects. Its conformational constraints allow detailed investigation of hydrogen bonding patterns, ring strain, and the influence of side chain composition on peptide geometry. Such studies are instrumental in advancing the understanding of peptide behavior in solution and solid states, informing the rational design of cyclic peptides with desired structural and functional characteristics.
1. Cationic cell-penetrating peptides are potent furin inhibitors
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
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