MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH is a modular peptide-linker construct containing aromatic and glycine-rich residues for flexible folding. The sequence aids in studying ligand tethering, peptide-protein interactions, and aromatic packing. Researchers use it to investigate spacer effects and conformational dynamics. Its terminal linker provides anchoring versatility.
CAT No: R2233
CAS No:1599440-25-1
Synonyms/Alias:MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH;1599440-25-1;(S)-10-Benzyl-23-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)-6,9,12,15,18-pentaoxo-3-oxa-5,8,11,14,17-pentaazatricosan-1-oic acid;MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH (GMP);2-[[[2-[[(2S)-2-[[2-[[2-[6-(2,5-dioxopyrrol-1-yl)hexanoylamino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]methoxy]acetic acid;SCHEMBL17003582;EX-A4328;ZNC44025;AKOS040756914;HY-131990G;BP-29530;DA-55281;MS-30749;HY-131990;CS-0145893;CS-0899296;F81359;Mal-Gly-Gly-L-Phe-N-[(carboxymethoxy)methyl]Glycinamide;Glycinamide,N-[6-(2,5-dihydro-2,5-dioxo-1H-pyrrol-1-yl)-1-oxohexyl]glycylglycyl-L-phenylalanyl-N-[(carboxymethoxy) methyl] -;
MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH is a synthetic carbohydrate-peptide conjugate designed to bridge the functional characteristics of both peptide and carbohydrate moieties. This compound features a peptide backbone composed of glycine and phenylalanine residues, linked to a modified carbohydrate chain, which imparts unique physicochemical properties. The structural configuration of MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH allows for enhanced solubility, stability, and specific molecular recognition capabilities, making it an attractive candidate for a variety of biochemical and research applications. Its amphiphilic nature and tailored terminal groups facilitate interactions with both hydrophilic and hydrophobic environments, broadening its utility across multiple scientific domains.
Peptide-carbohydrate interaction studies: MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH serves as a valuable model compound for investigating the intricate interactions between peptides and carbohydrates. By incorporating both peptide and carbohydrate elements, it provides a platform for elucidating the mechanisms underlying molecular recognition, binding affinities, and conformational changes that occur during such interactions. Researchers can utilize this conjugate in binding assays or structural studies to better understand the role of glycopeptide motifs in biological systems, which is critical for advancing knowledge in fields such as glycomics and proteomics. The compound's defined sequence and functional groups enable precise mapping of interaction sites, supporting the rational design of biomimetic molecules and inhibitors.
Bioconjugation and linker chemistry: The unique structure of MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH makes it an excellent scaffold for bioconjugation studies. Its terminal functional groups allow for facile chemical modification, enabling the attachment of fluorescent tags, affinity labels, or other biomolecules. This capability is particularly useful in the development of novel probes for imaging, tracking, or isolating specific biomolecular targets. By serving as a linker between different molecular entities, the compound can facilitate the creation of multifunctional bioconjugates, which are essential tools in analytical biochemistry and molecular biology research. Scientists can exploit its modular design to customize linkers for specific applications, thereby improving the efficiency and specificity of labeling or targeting strategies.
Enzyme substrate research: MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH is frequently utilized as a synthetic substrate in enzyme activity assays, especially for enzymes that recognize peptide-carbohydrate conjugates. Its well-defined structure allows for the systematic study of enzyme specificity, kinetics, and catalytic mechanisms. By varying the sequence or carbohydrate component, researchers can investigate structure-activity relationships and identify key determinants of enzyme recognition. This approach is instrumental in the discovery and characterization of novel enzymes, as well as in the optimization of enzymatic reactions for biotechnological applications.
Drug delivery system development: The amphiphilic and modular nature of MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH lends itself to the design of advanced drug delivery systems. Its ability to interact with both hydrophilic and hydrophobic molecules enables the formation of self-assembled structures such as micelles or nanoparticles, which can encapsulate therapeutic agents. By leveraging its peptide and carbohydrate domains, researchers can engineer delivery vehicles with improved targeting, stability, and controlled release properties. These systems are particularly relevant in the development of next-generation delivery platforms for small molecules, peptides, or nucleic acids, facilitating enhanced bioavailability and efficacy in preclinical research models.
Analytical method development: The defined composition and functional versatility of MC-Gly-Gly-Phe-Gly-NH-CH2-O-CH2COOH make it a valuable reference standard in the development and validation of analytical techniques. It can be employed in chromatographic, spectroscopic, or mass spectrometric methods to calibrate instruments, optimize separation conditions, or evaluate detection limits for glycopeptide analysis. The compound's stability and reproducibility ensure reliable performance in method development, supporting rigorous quality control and standardization efforts in research laboratories. By serving as a benchmark molecule, it aids in the advancement of sensitive and accurate analytical workflows for the detection and quantification of complex biomolecules.
1. High fat diet and GLP-1 drugs induce pancreatic injury in mice
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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