This modified lysine analog includes multiple protective groups and a cyclohexenone-derived substituent that affects steric bulk and electron distribution. The extended side chain allows exploration of metal coordination, conjugation chemistry, and conformational restriction. Researchers employ it in peptidomimetic scaffolding. Its dual protection facilitates selective transformations.
CAT No: R2146
CAS No:1428229-84-8
Synonyms/Alias:N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(2-hydroxy-4,4-dimethyl-6-oxocyclohex-1-en-1-yl)ethylidene)-N2-methyl-L-lysine;1428229-84-8;N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(2-hydroxy-4,4-dimethyl-6-oxocyclohex-1-en-1-yl)ethylidene)-N2-methyl-L-lysine;Fmoc-MeLys(Dde);AKOS030212444;(2S)-2-[9H-Fluoren-9-ylmethoxycarbonyl(methyl)amino]-6-[1-(2-hydroxy-4,4-dimethyl-6-oxocyclohexen-1-yl)ethylideneamino]hexanoic acid;
N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(2-hydroxy-4,4-dimethyl-6-oxocyclohex-1-en-1-yl)ethylidene)-N2-methyl-L-lysine is a highly specialized carbohydrate compound designed for advanced research applications in the fields of peptide synthesis, chemical biology, and molecular modification. Its unique structure, featuring both a fluorenylmethyloxycarbonyl (Fmoc) protecting group and a modified lysine residue with a cyclohexenone moiety, offers researchers a versatile building block for the creation of complex biomolecules. The presence of both hydrophobic and hydrophilic domains within the molecule allows for precise modulation of peptide properties, making it particularly suitable for studies that require site-specific modifications and enhanced molecular stability. The compound's chemical features enable selective reactions, facilitating the introduction of novel functional groups or labels at defined positions within peptides or proteins.
Peptide Synthesis: N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(2-hydroxy-4,4-dimethyl-6-oxocyclohex-1-en-1-yl)ethylidene)-N2-methyl-L-lysine serves as a valuable amino acid derivative in solid-phase peptide synthesis (SPPS). Its Fmoc-protected lysine backbone ensures compatibility with standard Fmoc/tBu chemistry, while the unique side-chain modification provides an orthogonal handle for subsequent conjugation or derivatization. Researchers can incorporate this compound into peptide chains to introduce site-specific modifications, such as fluorescent tags, affinity labels, or cross-linking moieties, enabling the study of protein-protein interactions, conformational dynamics, or molecular recognition events. The compound's stability under typical deprotection and coupling conditions further enhances its utility in generating high-purity, functionally diverse peptides.
Site-Specific Labeling: The modified lysine derivative is particularly advantageous for site-specific labeling strategies in chemical biology. The cyclohexenone functionality on the side chain can serve as a reactive site for selective conjugation with nucleophiles or other chemical probes. This enables the targeted introduction of biophysical reporters, such as fluorophores or spin labels, at precise locations within peptides or proteins. Such labeling is crucial for advanced spectroscopic studies, including fluorescence resonance energy transfer (FRET), electron paramagnetic resonance (EPR), and single-molecule tracking, where spatial resolution and specificity are paramount. The orthogonal reactivity of the side chain ensures minimal interference with other functional groups, supporting high-fidelity labeling even in complex biomolecular assemblies.
Protein Engineering: Incorporation of this methylated, cyclohexenone-modified lysine analog into recombinant proteins or synthetic peptides allows researchers to explore the effects of noncanonical amino acids on protein structure and function. By substituting the natural lysine residue with this analog, scientists can systematically investigate the impact of altered side-chain properties on enzymatic activity, protein folding, or intermolecular interactions. Such studies are instrumental in the rational design of proteins with enhanced stability, altered binding affinities, or novel catalytic activities. The compound's compatibility with genetic code expansion and chemical ligation techniques further broadens its applicability in protein engineering and synthetic biology.
Chemical Probe Development: The unique chemical features of N2-methyl-L-lysine derivatives make them attractive scaffolds for the development of selective chemical probes. The cyclohexenone moiety provides a versatile reactive handle for the attachment of reporter groups, affinity tags, or photoactivatable cross-linkers. These probes can be employed to map protein-protein or protein-ligand interactions, identify post-translational modification sites, or monitor dynamic changes in cellular environments. The modularity of the compound allows for the rapid generation of probe libraries tailored to specific biological questions, accelerating the discovery of novel molecular targets and pathways.
Bioconjugation and Therapeutic Delivery: The dual functionality of the Fmoc group and the modified lysine side chain enables efficient bioconjugation strategies for the attachment of peptides to other biomolecules, nanoparticles, or drug carriers. By leveraging its orthogonal reactivity, researchers can design multifunctional conjugates for targeted delivery, imaging, or therapeutic applications. The robust chemical stability and selective reactivity of the compound ensure that conjugation proceeds efficiently without compromising the integrity of sensitive payloads. This opens new avenues for the development of advanced delivery systems, biosensors, and diagnostic tools in biomedical research.
Synthetic Biology and Advanced Biomaterials: The integration of this modified lysine analog into synthetic peptides or protein-based materials allows for the creation of novel biomaterials with tunable properties. Its unique side-chain functionality can be exploited to introduce cross-linking sites, responsive elements, or bioactive motifs, enabling the design of smart hydrogels, self-assembling nanostructures, or functionalized surfaces. Such materials have significant potential in tissue engineering, regenerative medicine, and biosensing, where precise control over molecular architecture and functionality is essential. By providing a versatile platform for molecular customization, N2-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N6-(1-(2-hydroxy-4,4-dimethyl-6-oxocyclohex-1-en-1-yl)ethylidene)-N2-methyl-L-lysine empowers researchers to push the boundaries of synthetic biology and materials science.
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. Myotropic activity of allatostatins in tenebrionid beetles
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