60687-34-5

Upstream product

• 60687-36-7 (R)-(1-aminoethyl)phosphonic acid 
• 501-53-1 benzyl chloroformate 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 59577-42-3 2-benzyloxycarbonyloxyimino-2-phenylacetonitrile 

Downstream Products

• 121843-86-5 (R)-benzyl 1-(monomethoxyphosphoryl)ethylcarbamate 
• 859830-11-8 N-carbobenzoxy-L,1-aminoethylphosphonate-β-D-galactopyranoside tetraacetate 
• 121843-85-4 (R)-1-(N-benzyloxycarbonylamino)ethylphosphonic acid dimethyl ester 
• 98857-08-0 diethyl (1R)-1-{[carbobenzyloxy]amino}ethylphosphonate 

Relevant academic research and scientific papers

Synthesis and biological analysis of novel glycoside derivatives of L-AEP, as targeted antibacterial agents

To develop targeted methods for treating bacterial infections, the feasibility of using glycoside derivatives of the antibacterial compound L-R-aminoethylphosphonic acid (L-AEP) has been investigated. These derivatives are hypothesized to be taken up by b

Optically active polyoxotungstates bearing chiral organophosphonate substituents

Divacant Keggin-type polyoxotungstates [γ-XW10O 36]8-with X = Si or Ge, were functionalized with chiral phosphoryl groups. The hybrid compounds [(RPO)2(γ-XW 10O36)]4- with R = N-

A mild and convenient oxidation of H-phosphinic acids

A new mild and convenient method of oxidation of H-phosphinic to the corresponding phosphonic acids was developed. Conversion of H-phosphinic acids into trivalent trimethylsilyl esters using hexamethyldisilazane, followed by their oxidation with air and subsequent methanolysis allowed obtaining the final compounds in good to excellent yields. The methodology was proved to be particularly useful for N-benzyloxycarbonyl-α-aminophosphinic acids. The scope and limitations of the reaction were additionally tested using a variety of both free and protected amino- and hydroxyphosphinates as substrates.

THERAPEUTICALLY USEFUL ANTIBACTERIAL COMPOUNDS

Disclosed is a compound which has antibiotic activity in vivo in a mammalian, preferably a human, subject, the compound comprising an uptake moiety linked to a bactericidal or bacteriostatic toxic moiety, said uptake moiety facilitating uptake of the comp

An investigation of antibody acyl hydrolysis catalysis using a large set of related haptens

An aspect of catalytic antibody research that receives little attention in the literature involves hapten systems that fail to elicit antibody catalysts despite a high affinity immune response and hapten designs that resemble those known to elicit catalysts. We have investigated a series of 12 phosphate and phosphonate haptens in a total of three animal systems. Dramatic and reproducible differences were observed in the catalytic activities of polyclonal antibodies elicited by the different haptens. A phosphate hapten with a phenyl ring on the side of the hapten opposite the linker elicited reproducibly high levels of polyclonal antibody catalytic activity. The other 11 haptens, most with benzyl groups on the side of the hapten opposite the linker, elicited immune responses in which catalytic activity was significantly weaker in terms of the level of observed catalytic activity, as well as frequency of elicited catalysts. Our results indicate that subtle features of transition state analogue hapten structure can have a dramatic and reproducible influence over the catalytic activity of elicited antibodies in related haptens. Whatever the explanation, subtle changes in mechanistic features due to altered leaving group ability/location or overall hapten flexibility, the comprehensive data presented here indicate that phenyl or 4-nitrophenyl leaving groups located opposite the hapten linker are to be preferred in order to elicit highly active antibody catalysts for acyl hydrolysis reactions. (C) 2000 Elsevier Science Ltd.

Relaxing substrate specificity in antibody-catalyzed reactions: Enantioselective hydrolysis of N-Cbz-amino acid esters

For a catalytic antibody to be generally useful for organic synthetic chemistry, it must be able to accept a broad range of substrates, yet retain high selectivity. In this work, we propose a hapten design to endow antibody catalysts with two opposing qualities, such as high enantioselectivity and broad substrate specificity. Racemic hapten 2 induced two separate classes of catalytic antibodies to hydrolyze either the L- or D-isomers of N-Cbz-amino acid esters 1. In the kinetic resolution of racemic ester 9, antibodies 7G12 and 3G2 gave 96% ee of L-10 and 94% ee of D-10, respectively. In addition, antibody 7G12 displayed broad substrate specificity, hydrolyzing the L-esters of Ala (1a), Leu (1b), Norleu (1c), Met (1d), Phe (1e), Val (1f), and phenylglycine (1g) with high enantioselectivity. Antibody 3G2 also hydrolyzed the D-isomers of these esters without sacrificing the enantioselectivity. This observation suggests that the use of haptens that fit snugly into the antigen-combining site, and leave the linker moiety outside, is an effective approach for the generation of catalytic antibodies with high selectivity and broad substrate applicability.

Synthesis of α-aminophosphonic octapeptide, Phe-Gly-Ser-Leu-Ala(P)-Phl-Leu-Pro, an analog with partial sequence of erb B-2 gene product

A chemical synthesis was performed of an octapeptide with a phosphonic ester linkage, which corresponds to a variation of the partial sequence of a gene product of erb B-2. The phosphonic ester linkage was successfully prepared through a coupling reaction

Peptide derivatives of phosphonic and phosphinic acids and intermediates therefor

The present disclosure relates to peptide derivatives. More particularly, the disclosure is concerned with peptide derivatives of phosphonic and phosphinic acids, a process for the manufacture thereof and pharmaceutical preparations containing same.