Cyclo(-Gly-Trp) is a diketopiperazine formed from glycine and tryptophan, generating a compact ring that stabilizes aromatic-backbone interactions. Researchers use it to explore indole-associated folding, hydrophobic packing, and β-turn mimicry. Its rigidity supports detailed structural and mechanistic studies.
CAT No: R2295
CAS No:7451-73-2
Synonyms/Alias:Cyclo(-Gly-Trp);7451-73-2;Cyclo(glycyltryptophyl);(S)-3-((1H-Indol-3-yl)methyl)piperazine-2,5-dione;CHEBI:69031;(3S)-3-(1H-indol-3-ylmethyl)piperazine-2,5-dione;CYCLO(TRP-GLY);Cyclo(glycyl-L-tryptophan);Cyclo(-Trp-Gly);MFCD00083708;CHEMBL226544;SCHEMBL3120523;AS-87930;CS-0208968;G84179;Q27137374;
Cyclo(-Gly-Trp), also known as cyclo(glycyltryptophyl), is a cyclic dipeptide composed of glycine and tryptophan residues connected via a peptide bond forming a diketopiperazine ring structure. As a member of the diketopiperazine (DKP) family, this compound is recognized for its conformational rigidity, chemical stability, and unique physicochemical properties compared to linear peptides. Its structural motif is frequently encountered in natural products and bioactive molecules, making it a valuable scaffold in peptide chemistry, molecular recognition studies, and the development of functional biomaterials. The presence of both glycine and tryptophan within the cyclic framework contributes to its relevance in probing peptide folding, intermolecular interactions, and the design of peptide-based tools for biochemical research.
Peptide structure-activity relationship studies: Cyclo(-Gly-Trp) serves as a model compound in investigations of how cyclization influences peptide conformation and bioactivity. The diketopiperazine ring restricts the backbone flexibility, enabling researchers to systematically analyze the effects of conformational constraint on peptide-receptor interactions, stability against enzymatic degradation, and overall molecular recognition properties. Such studies inform the rational design of more stable and bioactive peptide analogs for research and industrial applications.
Molecular recognition and binding assays: The cyclic dipeptide structure of this compound makes it a useful probe for understanding non-covalent interactions such as hydrogen bonding, π-π stacking, and hydrophobic contacts in molecular recognition events. Its tryptophan side chain, with aromatic and indole functionalities, allows for the exploration of specific binding interactions with proteins, nucleic acids, or small molecules. These properties are particularly valuable in the development of peptide-based affinity reagents, sensors, or as competitors in binding assays.
Peptide-based materials research: Cyclo(-Gly-Trp) is utilized in the design and synthesis of peptide-based materials, including hydrogels and nanostructures. The inherent rigidity and propensity for self-assembly of diketopiperazines facilitate the formation of supramolecular architectures with tunable properties. Researchers exploit these features to investigate the self-assembly behavior of minimalistic peptide motifs and to develop novel biomaterials with potential applications in controlled release, surface modification, or as scaffolds for tissue engineering research.
Chemical synthesis and methodology development: The compound is often employed as a benchmark or intermediate in the development and optimization of synthetic methodologies for cyclic peptides. Its relatively simple structure and well-defined cyclization chemistry make it suitable for testing new cyclization strategies, protecting group manipulations, and analytical techniques such as NMR, mass spectrometry, and chromatography. These studies advance peptide synthesis protocols and facilitate the generation of more complex cyclic peptide libraries.
Analytical standard and reference compound: Due to its defined molecular structure and stability, cyclo(glycyltryptophyl) is frequently used as a reference standard in chromatographic and spectroscopic analyses. It supports the calibration of analytical instruments, validation of detection methods, and comparative studies involving related diketopiperazines or peptide fragments. Such applications are essential for ensuring data reliability in peptide research, quality control, and the characterization of novel cyclic peptides.
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