212140-39-1

Usage

Uses

Used in Pharmaceutical Industry:
N6-FMoc-D-lysine is used as a key building block for the synthesis of bioactive peptides and pharmaceuticals. Its unique structure allows for the introduction of lysine residues into peptides while protecting the amine group from unwanted reactions, facilitating the production of a wide range of therapeutic agents.
Used in Organic Chemistry:
In the field of organic chemistry, N6-FMoc-D-lysine is utilized as a versatile intermediate for the synthesis of various organic compounds. Its fluorine-modified 6-position and FMoc protecting group enable selective reactions and provide a stable platform for further functionalization.
Used in Solid-Phase Peptide Synthesis:
N6-FMoc-D-lysine is employed as a protected amino acid in solid-phase peptide synthesis. Its FMoc protecting group allows for efficient introduction of lysine residues into peptides, preventing side reactions and improving the overall yield and purity of the final product. This makes it an essential component in the development of peptide-based drugs and therapeutic agents.

Upstream product

• 28920-44-7 (9H-fluoren-9-yl)methyl azidoformate 
• 657-27-2 L-Lysine hydrochloride 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 84624-27-1 Boc-Lys(Fmoc)-OH 
• 56-87-1 L-lysine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 201009-98-5 N^ε-(9-fluorenylmethoxycarbonyl)-L-lysine methyl ester hydrochloride 
• 849752-39-2 6-(9H-fluoren-9-ylmethoxycarbonylamino)-2-[2-(4-trifluoromethyl-benzenesulfonyl)-ethoxycarbonylamino]-hexanoic acid methyl ester 
• 657-26-1 L-lysine dihydrochloride 

Downstream Products

• 183444-90-8 (S)-6-(9H-Fluoren-9-ylmethoxycarbonylamino)-2-{(S)-2-[(R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionylamino]-3-phenyl-propionylamino}-hexanoic acid 
• 186350-56-1 Alloc-L-Lys(N-Fmoc)-OH 
• 84624-27-1 Boc-Lys(Fmoc)-OH 

Relevant academic research and scientific papers

A lysoganglioside/poly-L-glutamic acid conjugate as a picomolar inhibitor of influenza hemagglutinin

Based on the principle of a multivalent interaction, the amphiphilic polymer 1, present in solution as an aggregate (see below right), is able to inhibit infection with the influenza virus. After recognition of a specific sialyllactose epitope through hemagglutinin (HA) on the virus surface, the sphingosine residues and the fluorescent tag form a stable complex with HA through hydrophobic interactions. Polymer 1 shows in vitro inhibitory activity 106-fold greater than that of sialyllactose. PGA = polyglutamic acid.

Chemistry in living cells: Detection of active proteasomes by a two-step labeling strategy

In vivo targeting of the proteasome: Probe 1 is a cell-permeable irreversible inhibitor that alkylates the active-site residues of the proteasome in a Michael fashion. After cell lysis, a biotin moiety is introduced by Staudinger ligation to yield construct 2. This strategy allows activity profiling of the catalytic activities of the proteasome in vivo.

Method for selective structural modification of L-lysine

The invention belongs to the field of chemical synthesis, and particularly relates to a method for selective structural modification of L-lysine. According to a specific technical scheme in the invention, L-lysine is taken as a raw material, silicon dioxide nanoparticles surface-functionalized by beta-cyclodextrin are taken as a catalyst, water is taken as a solvent, and a reaction is performed for 3-5 hours at 25 DEG C in the presence of an amino protective agent to obtain a final product of the reaction; the final reaction product is subjected to standing, and an upper-layer product is takenand subjected to washing, separating and filtering to obtain selectively-modified L-lysine. The used catalyst is odorless and non-toxic; the synthesis method is simple; catalytic performance is excellent; product separation is easy; the catalyst can be repeatedly used; the method effectively solves the problem that a mixture of a common beta-cyclodextrin catalyzed product and cyclodextrin floatson a liquid level and is difficult to separate, simplifies post-treatment steps, reduces the use amount of an organic solvent, and greatly reduces the amount of waste liquid generated in the stage ofpurification.

Decomposition of copper-amino acid complexes by oxalic acid dihydrate

A facile approach to the synthesis of some side-chain-protected amino acids via oxalic acid dihydrate as the copper sequestering reagent is presented. The copper in the amino acid complex reacted with oxalic acid dihydrate to form insoluble cupric oxalate, with the free amino acid released. Compared with conventional methods, this method is convenient, inexpensive, and environmentally friendly.

Decomposition of copper-amino acid complexes by sodium sulfide

Sodium sulfide very efficiently removes copper from protected amino acid-copper complexes. The copper in the amino acid complex was reduced to insoluble cuprous sulfide and the free amino acid was released in pure form. This method is very convenient and rapid, requiring only 5-10 min and 0.55-0.75 equiv of sodium sulfide.

Orthogonality and compatibility between Tsc and Fmoc amino-protecting groups

New deprotection conditions that provide a complete orthogonality between Tsc and Fmoc amino-protecting groups are described. The potential of these orthogonal deprotection conditions was then demonstrated by the efficient solid-phase synthesis of branched peptides 20 and 21 using doubly protected amino acids such as Tsc-Lys(Fmoc)-OH 4c and Fmoc-Lys(Tsc)-OH 4d.

Convenient Syntheses of Fluorenylmethyl-Based Side Chain Derivatives of Glutamic and Aspartic acids, Lysine and Cysteine

Efficient and practical one-pot syntheses of the fluorenylmethyl-based side chain derivatives of glutamic and aspartic acids, lysine, and cysteine are described.Likewise, stability/lability of these derivatives towards solvents and reagents used in solid