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1.
Org Biomol Chem ; 20(48): 9722-9733, 2022 12 14.
Article in English | MEDLINE | ID: mdl-36440712

ABSTRACT

A mild and efficient transition-metal-free radical difluorobenzylation/cyclization of unactivated alkenes toward the synthesis of difluorobenzylated polycyclic quinazolinone derivatives with easily accessible α,α-difluoroarylacetic acids has been developed. This transformation has the advantages of wide functional group compatibility, a broad substrate scope, and operational simplicity. This methodology provided a highly attractive access to pharmaceutically valuable ArCF2-containing polycyclic quinazolinones.


Subject(s)
Alkenes , Transition Elements , Cyclization , Quinazolinones , Molecular Structure , Free Radicals
2.
Guang Pu Xue Yu Guang Pu Fen Xi ; 29(4): 1060-3, 2009 Apr.
Article in Chinese | MEDLINE | ID: mdl-19626903

ABSTRACT

The interaction of genistein and human serum albumin (HSA) was investigated by fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet absorption spectra. The results showed that the quenching mechanism of the intrinsic fluorescence of HSA by genistein is due to the formation of genistein-HSA complex, resulting in a static quenching procedure. The binding constants (KA) were 1.00 x 10(6) (27 degrees C), 1.66 x 10(6) (37 degrees C) and 5.25 x 10(6) (47 degrees C), respectively. According to the Förster theory of non-radiation energy transfer, the binding distances (r) were 2.59 nm (27 degrees C), 2.65 nm (37 degrees C) and 2.90 nm (47 degrees C), respectively. The thermodynamic parameters showed that the binding power between genistein and HSA is mainly the electrostatic interaction Synchronous spectrum was used to investigate the conformational change of HSA.


Subject(s)
Genistein/chemistry , Phytoestrogens/chemistry , Serum Albumin/chemistry , Spectrometry, Fluorescence/methods , Humans , Kinetics , Protein Binding
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