684270-46-0

Usage

Uses

Used in Pharmaceutical Industry:
(S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID is used as a general N-terminal protected reagent for solid phase peptide synthesis. The azido group allows it to undergo copper-mediated click chemistry reactions, which are essential for the development of novel pharmaceutical compounds.
Used in Synthesis of Antifreeze Glycopeptides (AFGPs):
In the field of biochemistry, (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID is employed in the synthesis of α-N-acetylgalactosamine (α-GalNAc) linked antifreeze glycopeptides (AFGPs). These AFGPs exhibit unique properties that enable them to prevent ice crystal growth, making them valuable for various biotechnological and pharmaceutical applications.
Used in Drug Delivery Applications:
(S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID is also utilized in the synthesis of stimuli-responsive multifunctional peptide gatekeepers for drug delivery applications. These gatekeepers can control the release of drugs in response to specific stimuli, such as changes in pH, temperature, or the presence of certain molecules, thereby improving the efficacy and specificity of drug delivery systems.
Used in Synthesis of Triazole-Linked Glycopeptides:
Furthermore, (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID is used in the synthesis of triazole-linked glycopeptides via Cu(I)-catalyzed 1,3-dipolar cycloaddition (CuAAC). This method allows for the creation of complex and functionalized glycopeptides with potential applications in drug development, diagnostics, and therapeutics.

Upstream product

• 684270-35-7 (9H-fluoren-9-yl)methyl (S)-(3-hydroxy-1-(methoxy(methyl)amino)-1-oxopropan-2-yl)carbamate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 108492-14-4 tert-butyl (S)-3-azido-2-((tert-butoxycarbonyl)amino)propanoate 
• 122225-54-1 (S)-3-azido-2-((tert-butoxycarbonyl)amino)propanoic acid 
• 71989-16-7 Fmoc-Asn-OH 
• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 82911-78-2 N-[(9-fluorenylmethoxy)carbonyl]-L-serine methyl ester 
• 684270-41-5 [2-azido-1-(methoxy-methyl-carbamoyl)-ethyl]-carbamic acid 9H-fluoren-9-ylmethyl ester 

Downstream Products

• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 

Relevant academic research and scientific papers

Copper-Free Solid-Phase Synthesis of Triazolo[1,5-a][1,4]diazepin-6-ones

Synthesis of triazolo[1,5-a][1,4]diazepin-6-ones on solid support is reported in this article. Amino acids immobilized on Wang resin were nosylated and alkylated with propargyl alcohol, but-2-yn-1-ol or different 3-phenylprop-2-yn-1-ols using Mitsunobu alkylation conditions. After denosylation, acylation with Fmoc-azidoalanine yielded linear precursors that were thermally cyclized on resin to give immobilized triazolodiazepinones. After cleavage from the polymer support, the target compounds were obtained in high crude purities and good overall yields. Furthermore, the synthetic approach was applied to convenient solid-phase synthesis of oligopeptide containing the triazolodiazepinone moiety as the peptidomimetic heterocyclic constraint. (Figure presented.).

Highly potent and selective aryl-1,2,3-triazolyl benzylpiperidine inhibitors toward butyrylcholinesterase in Alzheimer's disease

Acetylcholinesterase (AChE) is the key enzyme targeted in Alzheimer's disease (AD) therapy, nevertheless butyrylcholinesterase (BuChE) has been drawing attention due to its role in the disease progression. Thus, we aimed to synthesize novel cholinesterases inhibitors considering structural differences in their peripheral site, exploiting a moiety replacement approach based on the potent and selective hAChE drug donepezil. Hence, two small series of N-benzylpiperidine based compounds have successfully been synthesized as novel potent and selective hBuChE inhibitors. The most promising compounds (9 and 11) were not cytotoxic and their kinetic study accounted for dual binding site mode of interaction, which is in agreement with further docking and molecular dynamics studies. Therefore, this study demonstrates how our strategy enabled the discovery of novel promising and privileged structures. Remarkably, compound 11 proved to be one of the most potent (0.17 nM) and selective (>58,000-fold) hBuChE inhibitor ever reported.

Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides

The rise of CuI-catalyzed click chemistry has initiated an increased demand for azido and alkyne derivatives of amino acid as precursors for the synthesis of clicked peptides. However, the use of azido and alkyne amino acids in peptide chemistry is complicated by their high cost. For this reason, we investigated the possibility of the in-house preparation of a set of five Fmoc azido amino acids: β-azido l-alanine and d-alanine, γ-azido l-homoalanine, δ-azido l-ornithine and ω-azido l-lysine. We investigated several reaction pathways described in the literature, suggested several improvements and proposed several alternative routes for the synthesis of these compounds in high purity. Here, we demonstrate that multigram quantities of these Fmoc azido amino acids can be prepared within a week or two and at user-friendly costs. We also incorporated these azido amino acids into several model tripeptides, and we observed the formation of a new elimination product of the azido moiety upon conditions of prolonged couplings with 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate/DIPEA. We hope that our detailed synthetic protocols will inspire some peptide chemists to prepare these Fmoc azido acids in their laboratories and will assist them in avoiding the too extensive costs of azidopeptide syntheses. Experimental procedures and/or analytical data for compounds 3–5, 20, 25, 26, 30 and 43–47 are provided in the supporting information.

Development of Cell-Permeable, Non-Helical Constrained Peptides to Target a Key Protein–Protein Interaction in Ovarian Cancer

There is a lack of current treatment options for ovarian clear cell carcinoma (CCC) and the cancer is often resistant to platinum-based chemotherapy. Hence there is an urgent need for novel therapeutics. The transcription factor hepatocyte nuclear factor

Noncovalent template-assisted mimicry of multiloop protein surfaces: Assembling discontinuous and functional domains

We report here a novel noncovalent synthetic strategy for template-assembled de novo protein design. In this approach, a peptide was first conjugated with two oligoguanosine strands via click chemistry and the conjugates were then self-assembled in the presence of metal ions. G-quadruplex formation directs two peptide strands to assemble on one face of the scaffold and form an adjacent two loop surface. This approach can be used to rapidly prepare multiple two-loop structures with both homo- and heterosequences.

Efficient synthesis of Fmoc-protected azido amino acids

The efficient two-step synthesis of Fmoc-protected L-azidoalanine and L-azidohomoalanine from readily available Fmoc-protected asparagine and glutamine, respectively, is reported. The synthetic route proceeds in good yield, requires no extra purification steps, and can be carried out on gram scale. The resulting azido amino acids are of sufficient purity for solid-phase peptide synthesis, as demonstrated in the synthesis of a model pentapeptide. Georg Thieme Verlag Stuttgart New York.

A short synthetic approach to chiral serine azido derivatives

We report a new synthetic methodology for the synthesis of chiral serine azido derivatives through a conversion of N-protected (Boc, Cbz and Fmoc) serine amino acid into its corresponding Weinreb amide. Thus, acidity of the α-proton of the serine is reduced and it allows nucleophilic addition reaction onto Weinreb amide to furnish chiral serine azido derivatives.