Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3

Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3 connects an Fmoc-protected tetrapeptide to an esterified linker for versatile synthetic modification. Researchers evaluate its role in resin-bound elongation and fragment condensation. The sequence offers balanced flexibility and aromatic interaction potential. Applications include peptide scaffold design, synthetic optimization, and linker engineering.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3(CAS 2866301-96-2)

CAT No: R2483

CAS No:2866301-96-2

Synonyms/Alias:Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3;2866301-96-2;SCHEMBL25412858;(S)-11-Benzyl-1-(9H-fluoren-9-yl)-3,6,9,12,15-pentaoxo-2-oxa-4,7,10,13,16-pentaazaheptadecan-17-yl acetate;HY-49412;CS-0775791;G79951;

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M.F/Formula
C33H35N5O8
M.W/Mr.
629.7
Sequence
One Letter Code:GGFG

Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3, a synthetic carbohydrate-peptide conjugate, represents a valuable tool in modern molecular research and development. Characterized by the presence of an Fmoc-protected N-terminus, a tetrapeptide backbone, and a modified C-terminal amide linked to an acetoxymethyl group, this compound offers unique chemical versatility. Its structure enables selective deprotection, straightforward incorporation into solid-phase synthesis protocols, and compatibility with a variety of analytical techniques. The combination of glycine and phenylalanine residues imparts both flexibility and aromatic interaction potential, making it suitable for diverse biochemical investigations. Researchers value its robust stability and adaptability in constructing complex biomolecules or studying peptide-carbohydrate interactions at a molecular level.

Peptide Synthesis: In the field of peptide synthesis, Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3 serves as an advanced building block for the assembly of peptide-based biomolecules. The Fmoc-protecting group ensures orthogonality in stepwise solid-phase peptide synthesis, allowing precise elongation of peptide chains. Its C-terminal modification facilitates the introduction of novel functionalities or linkers, making it well-suited for generating peptide conjugates or libraries with tailored properties. Researchers can leverage its structure to explore sequence-activity relationships or to develop custom peptides for biochemical assays, protein engineering, or bioactive compound screening.

Bioconjugation Studies: The unique acetoxymethyl modification at the C-terminus of this compound provides a reactive handle for bioconjugation strategies. Scientists utilize it to attach peptides to various biomolecules, surfaces, or reporter groups, thereby creating multifunctional probes or targeted delivery systems. Its compatibility with common coupling chemistries, such as amide bond formation or click reactions, streamlines the synthesis of peptide conjugates. This enables the study of protein-protein interactions, the design of biosensors, or the fabrication of peptide-functionalized materials for diagnostic and analytical applications.

Structural Biology: Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3 is employed in structural biology to investigate peptide folding, molecular recognition, and intermolecular interactions. The inclusion of glycine and phenylalanine residues offers a balance between conformational flexibility and aromatic stacking, making it an attractive model for studying secondary structure formation. Researchers can incorporate this compound into larger peptide constructs or use it as a reference standard in spectroscopic or crystallographic analyses. Insights gained from such studies contribute to the understanding of protein folding mechanisms and the rational design of peptide-based therapeutics or materials.

Material Science: In material science research, this peptide-carbohydrate conjugate is used to develop functionalized surfaces, hydrogels, or nanomaterials. Its chemical structure enables covalent attachment to polymers or inorganic substrates, imparting bioactivity or selective binding properties. Scientists exploit its modularity to fabricate biomimetic coatings, scaffolds for tissue engineering, or platforms for controlled drug delivery. The presence of aromatic and glycine residues enhances interactions with a range of biological and synthetic matrices, expanding its utility in designing advanced biomaterials.

Analytical Method Development: Analytical chemists harness the unique properties of Fmoc-Gly-Gly-Phe-Gly-NH-CH2-O-CO-CH3 for method development and validation. Its defined structure and predictable behavior during chromatographic separation, mass spectrometry, or electrophoresis make it an ideal standard or probe. The compound can be used to optimize detection protocols, evaluate peptide labeling strategies, or calibrate analytical instruments. By integrating it into assay development workflows, researchers ensure reliable quantification and characterization of peptides or related biomolecules, thereby enhancing the reproducibility and accuracy of analytical measurements.

InChI
InChI=1S/C33H35N5O8/c1-21(39)46-20-37-30(41)16-35-32(43)28(15-22-9-3-2-4-10-22)38-31(42)18-34-29(40)17-36-33(44)45-19-27-25-13-7-5-11-23(25)24-12-6-8-14-26(24)27/h2-14,27-28H,15-20H2,1H3,(H,34,40)(H,35,43)(H,36,44)(H,37,41)(H,38,42)/t28-/m0/s1
InChI Key
XWQQDGZCBPDSMX-NDEPHWFRSA-N

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