127903-20-2

Basic information

• Product Name: 6-(FMOC-AMINO)-1-HEXANOL
• Synonyms: (9H-fluoren-9-yl)Methyl (6-hydroxyhexyl)carbaMate;6-Fmoc-Acp-OL;Fmoc-Acp-OL;6-(Fmoc-amino)-1-hexanol≥ 98% (HPLC);FMOC-ACP(6)OL;FMOC-6-AMINOHEXANOL;FMOC-NH-(CH2)6-OH;6-(FMOC-AMINO)-1-HEXANOL
• CAS NO: 127903-20-2
• Molecular Formula: C₂₁H₂₅NO₃
• Molecular Weight: 339.43
• Mol File: 127903-20-2.mol
• Article Data: 13

Chemical Properties

• Melting Point: 119 °C
• Boiling Point: 539.2 °C at 760 mmHg
• Flash Point: 279.9 °C
• Appearance: /
• Density: 1.151 g/cm³
• Vapor Pressure: 1.86E-12mmHg at 25°C
• Refractive Index: 1.578
• Storage Temp.: 2-8°C
• BRN: 4531101
• CAS DataBase Reference: 6-(FMOC-AMINO)-1-HEXANOL(CAS DataBase Reference)
• NIST Chemistry Reference: 6-(FMOC-AMINO)-1-HEXANOL(127903-20-2)
• EPA Substance Registry System: 6-(FMOC-AMINO)-1-HEXANOL(127903-20-2)

Safety Data

• Hazard Codes: Xi
• Safety Statements: S24/25:Avoid contact with skin and eyes.
• WGK Germany: 3
• Hazardous Substances Data: 127903-20-2(Hazardous Substances Data)

Usage

Chemical Properties

White to off-white powder

Uses

Reagent for the introduction of a spacer arm

InChI:InChI=1/C21H25NO3/c23-14-8-2-1-7-13-22-21(24)25-15-20-18-11-5-3-9-16(18)17-10-4-6-12-19(17)20/h3-6,9-12,20,23H,1-2,7-8,13-15H2,(H,22,24)

Upstream product

• 4048-33-3 6-amino-1-hexanol 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 629-11-8 1,6-hexanediol 
• 742103-41-9 6-[(4-methoxy-phenyl)-diphenyl-methoxy]-hexan-1-ol 
• 88574-06-5 6-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}hexanoic acid 
• 1308344-03-7 (9H-fluoren-9-yl)methyl (6-((4-methoxybenzyl)oxy)hexyl)carbamate 
• 1308344-14-0 C₁₄H₂₃NO₂ 

Downstream Products

• 290308-58-6 Succinic acid benzyl ester (2R,3R,4R,5R,6R)-3,4-diacetoxy-5-acetylamino-6-[6-(9H-fluoren-9-ylmethoxycarbonylamino)-hexyloxy]-tetrahydro-pyran-2-ylmethyl ester 
• 952661-18-6 2-benzyl-3-oxo-(2-oxo-2-phenylethoxy)propyl{1-[(9H-fluoren-9-ylmethoxy)carbonyl]-2-azepanyl}phosphinic acid 
• 952661-13-1 2-benzyl-3-[{1-[(9H-fluoren-9-ylmethoxy)carbonyl]-2-azepanyl}(hydroxy)phosphoryl]propanoic acid 
• 134939-08-5 VO(OCH₂CH(CH₃)2)2(OC₆H₄NH₂) 

Relevant articles and documents

A facile synthesis of ω-aminoalkyl ammonium hydrogen phosphates

A series of ω-aminoalkyl ammonium hydrogen phosphates were synthesized through a simple and efficient three-step method. The starting materials, ω-aminoalkyl alcohols (AC-n, with carbon number n = 3, 4, 5, 6), were amino-protected with 9-fluorenylmethyl chloroformate (Fmoc-Cl), followed by phosphorylation with POCl3 and deprotection in piperidine/DMF. The structures of each intermediate and final product were confirmed by 1H NMR, FTIR and mass spectrum. The yield of each step was about 77-92%, with a total yield higher than 56%. This new method was superior in low-cost raw materials, mild reaction temperatures (0-25°C) and easy purification methods.

Preparation method of triphosphate compound and deoxynucleotide

The invention discloses a preparation method of a triphosphate compound and deoxynucleotide. In the preparation method of the triphosphate compound, tetrahydrofuran is used for replacing trimethyl phosphate/triethyl phosphate, tri-n-propylamine is used for replacing tri-n-butylamine, and acetonitrile is used for replacing N,N-dimethylformamide; so that the preparation method has the advantages that the yield is high, few byproducts are produced, a solvent is easy to remove, and the triphosphate compound is non-toxic, safe and the like. According to the preparation method of the deoxynucleotide, the morpholine dimethylformamide solution is used for replacing a triethylamine solution to remove the F-moc group, so that the reaction time is greatly shortened, the generation of byproducts is reduced, and the yield is improved.

Extracellular targeted drug conjugates

The present invention relates to, inter alia, extracellular drug conjugates (EDC) in which an antibody or other targeting agent (e.g. a targeting moiety) is linked to a drug through a linker (e.g. a non-cleavable linker). These conjugates are useful in the treatment of disease and/or as a tool in the evaluation of biological systems.

Elucidation of the active conformation of vancomycin dimers with antibacterial activity against vancomycin-resistant bacteria

Covalently linked vancomycin dimers have attracted a great deal of attention among researchers because of their enhanced antibacterial activity against vancomycin-resistant strains. However, the lack of a clear insight into the mechanisms of action of these dimers hampers rational optimization of their antibacterial potency. Here, we describe the synthesis and antibacterial activity of novel vancomycin dimers with a constrained molecular conformation achieved by two tethers between vancomycin units. Conformational restriction is a useful strategy for studying the relationship between the molecular topology and biological activity of compounds. In this study, two vancomycin units were linked at three distinct positions of the glycopeptide (vancosamine residue (V), C terminus (C), and N terminus (N)) to form two types of novel vancomycin cyclic dimers. Active NC-VV-linked dimers with a stable conformation as indicated by molecular mechanics calculations selectively suppressed the peptidoglycan polymerization reaction of vancomycin-resistant Staphylococcus aureus in vitro. In addition, double-disk diffusion tests indicated that the antibacterial activity of these dimers against vancomycin-resistant enterococci might arise from the inhibition of enzymes responsible for peptidoglycan polymerization. These findings provide a new insight into the biological targets of vancomycin dimers and the conformational requirements for efficient antibacterial activity against vancomycin-resistant strains. Squashing superbugs: Conformationally constrained vancomycin dimers that inhibit the peptidoglycan synthesis of vancomycin-resistant bacteria were prepared (see scheme). The potent antibacterial activity of the dimers was suggested to arise from their direct action on transglycosylase enzymes. Copyright