268674
2-Aminoethylphosphonic acid
99%
Synonym(s):
2-AEP
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About This Item
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Assay
99%
form
solid
mp
296 °C (dec.) (lit.)
solubility
water: soluble 50 mg/mL, clear, colorless
functional group
amine
SMILES string
NCCP(O)(O)=O
InChI
1S/C2H8NO3P/c3-1-2-7(4,5)6/h1-3H2,(H2,4,5,6)
InChI key
QQVDJLLNRSOCEL-UHFFFAOYSA-N
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General description
The surface of gold nanoparticles (Au NPs) were functionalized with 2-aminoethylphosphonic acid that exhibited calcium affinity which enabled targeted delivery of Au NPs to calcified tissue.
Application
2-Aminoethylphosphonic acid was used as a growth medium for the marine bacterium Roseovarius nubinhibens ISM.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Biodegradation, 18(2), 223-231 (2006-06-08)
Air-born mixed fungal and bacterial culture capable of complete degradation of ciliatine was isolated. The utilization of the natural organophosphonate proceeded in the phosphate independent manner. Enzymatic activity involved in ciliatine degradation studied in the fungal cell-free extract proved to
Chemical communications (Cambridge, England), (7)(7), 878-879 (2003-05-13)
Carbon-supported catalysts were phosphonated using 2-aminoethylphosphonic acid, and the resulting catalysts with largely enhanced proton conductivity performed substantially better than the untreated counterparts in proton-exchange membrane fuel cells.
Biochemistry, 41(44), 13162-13169 (2002-10-31)
Phosphonates allow certain organisms to thrive in otherwise hostile environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate synthesis and degradation pathways. The crystal structure of AEP transaminase was
Synthesis of monensin derivatives and their effect on the activity of ricin A-chain immunotoxins.
Methods in molecular biology (Clifton, N.J.), 166, 55-70 (2001-02-24)
Acta crystallographica. Section F, Structural biology and crystallization communications, 64(Pt 5), 327-333 (2008-05-06)
Bacillus anthracis, the causative agent of anthrax, has been targeted by the Oxford Protein Production Facility to validate high-throughput protocols within the Structural Proteomics in Europe project. As part of this work, the structures of an alanine racemase (BA0252) in
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