684270-46-0

Basic information

• Product Name: (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID
• Synonyms: FMoc-β-azido-Ala-OH;FMOC-L-BETA-AZIDOALANINE;3-Azido-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine;FMoc-beta-azido-Ala-OH >=98.0% (HPLC);Fmoc-L-Dap(N3)-OH;3-Azido-N-Fmoc-L-alanine;Fmoc-L-Aza-OH;2-(S)-Fmoc-amino-3-azidopropanoic acid
• CAS NO: 684270-46-0
• Molecular Formula: C₁₈H₁₆N₄O₄
• Molecular Weight: 0
• Product Categories: amino acids;Fmoc Amino Acids;Fmoc-Amino Acids
• Mol File: 684270-46-0.mol
• Article Data: 7

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• Solubility: DMF (Slightly), DMSO (Slightly), Methanol (Slightly)
• CAS DataBase Reference: (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID(684270-46-0)
• EPA Substance Registry System: (S)-2-(((9H-FLUOREN-9-YL)METHOXY)CARBONYLAMINO)-3-AZIDOPROPANOIC ACID(684270-46-0)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26
• WGK Germany: 3
• Hazardous Substances Data: 684270-46-0(Hazardous Substances Data)

Usage

Chemical Properties

White to off-white crystalline powder

Uses

Fmoc-β-azido-Ala-OH chloride is a general N-terminal protected reagent used in the solid phase peptide synthesis. Azido group allows it to undergo copper-mediated click chemistry reactions.It can be used in:Synthesis of α-N-acetylgalactosamine (α-GalNAc) linked antifreeze glycopeptides (AFGPs).Synthesis of stimuli-responsive multifunctional peptide gatekeepers for drug delivery applications.Synthesis of triazole-linked glycopeptides via Cu(I)-catalyzed 1,3-dipolar cycloaddition (CuAAC).

Upstream product

• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 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 
• 684270-35-7 (9H-fluoren-9-yl)methyl (S)-(3-hydroxy-1-(methoxy(methyl)amino)-1-oxopropan-2-yl)carbamate 
• 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

• 1001094-10-5 C₂HF₃O₂*C₄₃H₄₈N₁₀O₉ 
• 1001094-07-0 C₂HF₃O₂*C₄₃H₄₆N₁₀O₁₀ 
• 1001094-32-1 C₂HF₃O₂*C₄₂H₄₆N₁₀O₁₀ 
• 1374243-98-7 (2S)-3-[4-(dibenzyl-phosphono)-[1,2,3]triazol-1-yl]-2-(9H-fluoren-9-ylmethoxycarbonyl)aminopropionic acid 
• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 

Relevant articles and documents

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.).

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.