N6-(Bis(ethylamino)methylene)-D-lysine is a modified lysine derivative introducing a bis(ethylamino) moiety for enhanced cationic character. The structural change supports studies of polyamine-like interactions and nucleic-acid binding. Researchers evaluate its conformational behavior and reactivity. Applications include peptide modification, charge-tuning studies, and polycationic motif design.
CAT No: R2593
CAS No:98500-82-4
Synonyms/Alias:N6-(Bis(ethylamino)methylene)-D-lysine;98500-82-4;D-Diethyl-homoarginine;BD645UH6BV;(2R)-2-amino-6-[bis(ethylamino)methylideneamino]hexanoic Acid;UNII-BD645UH6BV;D-Lysine, N6-(bis(ethylamino)methylene)-;N6-((Ethylamino)(ethylimino)methyl)-D-lysine;N6-?[Bis(ethylamino)?methylene]?-D-?lysine;FD164027;
N6-(Bis(ethylamino)methylene)-D-lysine is a synthetic amino acid derivative featuring a modified lysine backbone with a bis(ethylamino)methylene functional group at the N6 position. As a non-proteinogenic D-amino acid analog, it is distinguished by its unique side-chain modification, which imparts altered chemical reactivity and structural properties compared to its natural counterpart. This compound is of significant interest in biochemical research due to its potential to modulate peptide structure, facilitate site-specific labeling, and serve as a versatile building block in the synthesis of novel biomolecules. Its distinctive configuration and functionalization make it a valuable tool for investigating the effects of side-chain modifications on protein folding, molecular interactions, and enzymatic processes.
Peptide synthesis: The incorporation of N6-(Bis(ethylamino)methylene)-D-lysine into custom peptides provides researchers with a means to introduce site-specific chemical diversity into polypeptide sequences. Its modified side chain enables the design of peptides with enhanced stability, altered charge distribution, or tailored reactivity, supporting the development of novel biomaterials and functionalized peptides for in vitro studies. The D-configuration further contributes to proteolytic resistance, which is advantageous in the design of peptides intended for mechanistic or structural investigations where prolonged stability is required.
Protein engineering: In the context of protein engineering, this lysine analog can be strategically introduced into proteins to probe the influence of non-canonical side chains on protein folding, stability, and intermolecular interactions. By replacing natural lysine residues with this synthetic derivative, researchers can systematically investigate the role of side-chain charge, hydrogen bonding, and steric factors in protein architecture. Such studies are instrumental in elucidating structure-function relationships and guiding the rational design of proteins with improved or novel properties.
Chemical biology: The unique bis(ethylamino)methylene modification on the ε-amino group of lysine serves as a reactive handle for site-selective conjugation strategies. This property is particularly valuable in chemical biology applications where precise labeling, crosslinking, or immobilization of peptides and proteins is required. The compound enables the attachment of probes, affinity tags, or functional groups through chemoselective reactions, facilitating advanced studies in proteomics, molecular imaging, and bioanalytical assay development.
Enzyme substrate specificity studies: The use of N6-modified D-lysine analogs in enzyme assays allows researchers to explore the substrate specificity and catalytic mechanisms of lysine-processing enzymes, such as transaminases, oxidases, or methyltransferases. By assessing enzyme activity with this non-natural substrate, it is possible to delineate the structural requirements for substrate recognition and catalysis, advancing the understanding of enzyme selectivity and informing the design of enzyme inhibitors or engineered biocatalysts.
Structure-activity relationship (SAR) analysis: Incorporation of this synthetic amino acid into peptide libraries or protein variants supports systematic SAR studies aimed at mapping the contribution of lysine side-chain modifications to biological activity, binding affinity, or molecular recognition. Such investigations are essential in the development of peptide-based ligands, molecular probes, or biomimetic materials, providing insight into how subtle chemical changes can modulate biological function and molecular interactions.
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