MC-Gly-Gly-Phe combines a modular linking group with a flexible diglycine and an aromatic phenylalanine that shapes hydrophobic behavior. The construct supports investigations of cleavage sensitivity and enzymatic selectivity. Researchers evaluate its folding tendencies and solvent interactions. Use includes prodrug-model development, peptide synthesis studies, and mechanistic profiling.
CAT No: R2639
CAS No:1599440-15-9
Synonyms/Alias:MC-Gly-Gly-Phe;1599440-15-9;(2S)-2-[[2-[[2-[6-(2,5-dioxopyrrol-1-yl)hexanoylamino]acetyl]amino]acetyl]amino]-3-phenylpropanoic acid;MFCD32690114;SCHEMBL17003656;WLZ3750;DTXSID901130594;(2S)-2-(2-{2-[6-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanamido]acetamido}acetamido)-3-phenylpropanoic acid;EX-A5701;AKOS040743568;AC-32500;DA-65291;HY-44235;MS-28742;PD125818;CS-0106193;E79158;(6-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanoyl)glycylglycyl-L-phenylalanine;N-[6-(2,5-Dihydro-2,5-dioxo-1H-pyrrol-1-yl)-1-oxohexyl]glycylglycyl-L-phenylalanine;(S)-2-(2-(2-(6-(2,5-Dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanamido)acetamido)acetamido)-3-phenylpropanoic acid;
MC-Gly-Gly-Phe, also known as methylcarbamate-Gly-Gly-Phe, represents a specialized carbohydrate-peptide conjugate that has attracted significant interest in biochemical research and molecular design. Featuring a methylcarbamate moiety linked to a glycine-glycine-phenylalanine tripeptide, this compound exhibits unique physicochemical properties that enable its integration into various experimental systems. Its structure offers both hydrophilic and hydrophobic domains, making it an adaptable building block for exploring molecular recognition, enzymatic activity, and peptide-carbohydrate interactions. Researchers value MC-Gly-Gly-Phe for its versatility in synthetic chemistry and its potential to serve as a model compound in the development of novel biomaterials or analytical tools.
Peptide Substrate Design: MC-Gly-Gly-Phe is frequently employed as a model substrate in studies investigating the specificity and kinetics of peptidases and proteases. The presence of both glycine and phenylalanine residues allows for the assessment of enzyme-substrate interactions, particularly in the context of structure-activity relationship research. By incorporating this compound into enzymatic assays, scientists can elucidate the mechanisms of peptide bond cleavage and evaluate the influence of carbamate modifications on substrate recognition. Such insights are crucial for advancing our understanding of enzyme selectivity and for designing tailored inhibitors or substrates for biochemical applications.
Enzyme Inhibitor Screening: In the realm of drug discovery and biochemical screening, methylcarbamate-Gly-Gly-Phe serves as a valuable probe for identifying and characterizing protease inhibitors. Its defined sequence and functional groups make it suitable for high-throughput screening platforms, where it can be used to monitor the efficacy of potential inhibitory compounds. By tracking the hydrolysis or modification of this substrate in the presence of candidate molecules, researchers can rapidly assess inhibitor potency and selectivity, streamlining the early stages of lead optimization in pharmaceutical research.
Bioconjugation and Labeling: The distinct functional groups present in MC-Gly-Gly-Phe facilitate its use in bioconjugation strategies, particularly for the attachment of fluorescent tags, affinity labels, or other reporter molecules. Such modifications enable the creation of labeled peptides for use in imaging, detection, or quantification assays. The methylcarbamate group provides a convenient handle for chemical derivatization, expanding the utility of this compound in developing sensitive analytical methods or targeted delivery systems within complex biological environments.
Peptide-Based Material Science: Gly-Gly-Phe derivatives, including those featuring methylcarbamate protection, are increasingly explored in the design of peptide-based materials and hydrogels. Their inherent self-assembly properties, driven by aromatic and backbone interactions, can be fine-tuned through chemical modifications such as carbamoylation. This allows researchers to engineer novel biomaterials with controlled mechanical properties, responsiveness to external stimuli, or specific biofunctionalities. Applications range from scaffolds for tissue engineering to vehicles for controlled release of bioactive agents, highlighting the versatility of these peptide conjugates in material science.
Analytical Method Development: The unique structural features of MC-Gly-Gly-Phe render it an excellent standard or reference compound in the development of chromatographic and spectrometric analytical methods. Its predictable retention behavior and characteristic spectral signatures make it suitable for calibrating instruments, validating assay protocols, or benchmarking the performance of analytical platforms. By serving as a reliable reference, this compound supports the rigorous quality control and standardization required in advanced biochemical research and development laboratories.
MC-Gly-Gly-Phe thus stands out as a multifunctional tool in peptide chemistry, enzymology, analytical science, and material engineering. Its adaptable structure and chemical reactivity underpin a wide spectrum of research applications, from probing enzyme mechanisms and screening inhibitors to constructing novel biomaterials and refining analytical techniques. As scientific exploration continues to evolve, the diverse utility of this carbohydrate-peptide conjugate ensures its ongoing relevance in both fundamental and applied research settings.
4. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
5. The spatiotemporal control of signalling and trafficking of the GLP-1R
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