844697-83-2Relevant academic research and scientific papers
New reactions of selenocarboxylates
Knapp, Spencer,Darout, Etzer
, p. 203 - 206 (2005)
(Chemical Equation Presented) By treatment with Woollins' reagent in toluene solution, carboxylic acids are converted to selenocarboxylic acids. The latter react in situ to provide new products of acid- or base-promoted substitution, addition, and amidation.
Biohybrid-Se-S-coupling reactions of an amino acid derived seleninate
Abdo, Mohannad,Sun, Zhexun,Knapp, Spencer
, p. 1963 - 1972 (2013/04/24)
We describe the synthesis of the N-(2-seleninatoethyl) amide of N-Bocphenylalanine, serving here as a peptide model, and its reductive coupling reactions under mild conditions with unprotected thiouridine and glutathione. Selenosulfide products such as these comprise reversibly conjugated bio-components, and can potentially find uses as probes of biological function, such as enzyme inhibitors, delivery systems, or structural mimics.
Electrophilic aromatic selenylation: New OPRT inhibitors
Abdo, Mohannad,Zhang, Yong,Schramm, Vern L.,Knapp, Spencer
supporting information; experimental part, p. 2982 - 2985 (2010/11/19)
2-Ethoxyethaneseleninic acid reacts with electron-rich aromatic substrates to deliver, by way of the selenoxides, the (2-ethoxyethyl)seleno ethers, which can in turn be transformed into a diverse set of aryl-selenylated products. Among these, a family of 5-uridinyl derivatives shows submicromolar inhibition of human and malarial orotate phosphoribosyltransferase.
Biomimetic seleninates and selenonates
Abdo, Mohannad,Knapp, Spencer
supporting information; experimental part, p. 9234 - 9235 (2009/02/02)
The synthesis of a variety of pyranose-, nucleoside-, (amino acid)-, and polyhydric-based seleninic and selenonic acids by DMDO oxidation of the corresponding selenoesters is reported, as well as some unusual coupling reactions of the seleninate and selenonate functionality with biological nucleophilic groups (sulfhydryl, indole, phenol, imidazole, carboxamide) that are found in proteins and enzyme active sites. Copyright
Seleninate in place of phosphate: Irreversible inhibition of protein tyrosine phosphatases
Abdo, Mohannad,Liu, Sijiu,Zhou, Bo,Walls, Chad D.,Wu, Li,Knapp, Spencer,Zhang, Zhong-Yin
supporting information; experimental part, p. 13196 - 13197 (2009/02/06)
A homotyrosine based seleninic acid irreversibly inhibits protein tyrosine phosphatases by forming a covalent selenosulfide linkage with the active site cysteine sulfhydryl specifically. The details of the event are revealed by model synthetic studies and by kinetic, mass spectrometric, and crystallographic characterization. Copyright
