90763-54-5Relevant academic research and scientific papers
A One-Pot Conversion of α-Aminoalkylphosphonous Acids into Monomethyl α-Aminoalkylphosphonates
Strancar, Katja,Gobec, Stanislav
, p. 359 - 362 (2007/10/03)
An excellent method for a one-pot conversion of N-protected α-aminoalkylphosphonous acids into the corresponding monomethyl phosphonates, using thionyl chloride in methanol, has been devised. N-Protected monomethyl α-aminoalkylphosphonates are valuable intermediates in the preparation of phosphapeptides.
The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity
Grembecka, Jolanta,Mucha, Artur,Cierpicki, Tomasz,Kafarski, Pawe?
, p. 2641 - 2655 (2007/10/03)
A new class of very potent inhibitors of cytosol leucine aminopeptidase (LAP), a member of the metalloprotease family, is described. The X-ray structure of bovine lens leucine aminopeptidase complexed with the phosphonic acid analogue of leucine (LeuP) wa
Alkylation of potassium 1-(N-benzyloxycarbonyl-amino)alkylphosphonates and phosphinates in the presence of 18-crown-6
Skwarczynski,Kafarski
, p. 3565 - 3571 (2007/10/03)
During past several years we have been engaged in the synthesis of phosphono peptides, peptide analogues with phosphonic acid replacing C-terminal or N-terminal carboxylate moiety. These compounds are of interest not only because of their promise of direct practical applications but also as a source of information about mechanisms of enzymatic reactions. Esters of N-blocked 1-aminoalkylphosphonic and phosphinic acids are popularly used as starting substrates in multistep syntheses of phosphono peptides. Although several methods for their preparation have been described the search for the new and useful methods of their synthesis is still in progress. In this paper we report that the use of complexes of potassium 1-(N-benzyloxycarbonylamino)alkylphosphonates and phosphinates with 18-crown-6 as nucleophiles in the reaction with alkyl halides afforded the desired esters in good yields.
AN ANALYSIS OF THE ENZYME-INHIBITOR BINDING INTERACTIONS FOR PHOSPHONIC ACID TRANSITION STATE ANALOGS OF THERMOLYSIN
Bartlett, Paul A.,Marlowe, Charles K.
, p. 537 - 544 (2007/10/02)
Potent inhibitors of the zinc endopeptidase thermolysin are produced on replacement of the scissile peptide linkage with phosphonamidate or phosphonate ester moieties.These inhibitors have been shown to be transition state analogs, and a comparison betwee
