154109-03-2Relevant academic research and scientific papers
Phosphonic acid analogs of fluorophenylalanines as inhibitors of human and porcine aminopeptidases N: Validation of the importance of the substitution of the aromatic ring
Dziuk, B?a?ej,Kafarski, Pawe?,Pirat, Jean-Luc,Talma, Micha?,Wanat, Weronika
, (2020/05/04)
A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results from the placement of aromatic side chain of an inhibitor. Interestingly, both enantiomers of the individual compounds are usually bound quite similarly.
Studies on organophosphorus compounds; LXXV: A facile synthesis of 1-(hydroxyamino)alkyl(or aryl)phosphonic acids
Yuan,Chen,Zhou,Maier
, p. 955 - 957 (2007/10/02)
Reduction of dialkyl 1-(hydroxyimino)alkyl(aryl)phosphonate 1 with borane-pyridine complex proceeds smoothly to give dialkyl 1-(hydroxyamino)alkyl(or aryl)phosphonate 2 which is then easily converted into the corresponding hydroxyaminophosphonic acid 3 by
