6881-57-8Relevant articles and documents
Hydrolysis and alcoholysis of phosphinates and phosphonates
Harsági, Nikoletta,Keglevich, Gy?rgy,Sz?ll?si, Betti,Varga, Petra Regina
, (2021/11/04)
Phosphinic and phosphonic acids useful intermediates and biologically active compounds may be prepared from their esters: phosphinates and phosphonates, respectively, by acid-catalyzed hydrolysis either on conventional heating or on MW irradiation. The transesterification of alkyl phosphinates took place only in the presence of suitable ionic liquids as the catalysts. In the cases of phenylphosphonates, depending on the nature of the ionic liquid, the formation of the ester was accompanied by the fission of the C–O bond.
Synthesis and inhibitory activity of acetamidophosphonic acids against metallo-β-lactamases
Zhang, Yi-Lin,Zhang, Yue-Juan,Wang, Wen-Ming,Yang, Ke-Wu
, p. 14 - 18 (2016/12/24)
Metallo-β-lactamases (MβLs) are the target enzymes of antibiotic resistance and the phosphonic drugs make great influence to the development of contemporary medicine. Eleven acetamidophosphonic compounds were prepared and evaluated as inhibitors of the MβLs. Compounds 4, 5, 7, 9, and 10 exhibited specific inhibitory activity against the MβL NDM-1 and CcrA with an IC50 value range of 17 to 354 μM. Analysis of the structure–activity relationship showed that both the acetamido linker and the position of the substituent on the phenyl ring played an important role in the inhibitory abilities of the inhibitors against MβLs.
Crystal structures of the apo form and a complex of human LMW-PTP with a phosphonic acid provide new evidence of a secondary site potentially related to the anchorage of natural substrates
Fonseca, Emanuella M.B.,Trivella, Daniela B.B.,Scorsato, Valéria,Dias, Mariana P.,Bazzo, Natália L.,Mandapati, Kishore R.,De Oliveira, Fábio L.,Ferreira-Halder, Carmen V.,Pilli, Ronaldo A.,Miranda, Paulo C.M.L.,Aparicio, Ricardo
, p. 4462 - 4471 (2015/08/03)
Low molecular weight protein tyrosine phosphatases (LMW-PTP, EC 3.1.3.48) are a family of single-domain enzymes with molecular weight up to 18 kDa, expressed in different tissues and considered attractive pharmacological targets for cancer chemotherapy. Despite this, few LMW-PTP inhibitors have been described to date, and the structural information on LMW-PTP druggable binding sites is scarce. In this study, a small series of phosphonic acids were designed based on a new crystallographic structure of LMW-PTP complexed with benzylsulfonic acid, determined at 2.1 ?. In silico docking was used as a tool to interpret the structural and enzyme kinetics data, as well as to design new analogs. From the synthesized series, two compounds were found to act as competitive inhibitors, with inhibition constants of 0.124 and 0.047 mM. We also report the 2.4 ? structure of another complex in which LMW-PTP is bound to benzylphosphonic acid, and a structure of apo LMW-PTP determined at 2.3 ? resolution. Although no appreciable conformation changes were observed, in the latter structures, amino acid residues from an expression tag were found bound to a hydrophobic region at the protein surface. This regions is neighbored by positively charged residues, adjacent to the active site pocket, suggesting that this region might be not a mere artefact of crystal contacts but an indication of a possible anchoring region for the natural substrate - which is a phosphorylated protein.
