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Abstract
Thiol-functionalized silica nanospheres (SiO2-SH NSs) with an average diameter of 460 nm were synthesized through a hydrothermal route. Subsequently, the prepared SiO2-SH NSs were modified by SnO2 quantum dots to afford SnO2/SiO2 composite NSs possessing obvious fluorescence, which could be used to trace the target protein. The SnO2/SiO2 NSs were further modified by reduced glutathione (GSH) to obtain SnO2/SiO2-GSH NSs, which can specifically separate glutathione S-transferase-tagged (GST-tagged) protein. Moreover, the peroxidase activity of glutathione peroxidase 3 (GPX3) separated from SnO2/SiO2-GSH NSs in vitro was evaluated. Results show that the prepared SnO2/SiO2-GSH NSs exhibit negligible nonspecific adsorption, high concentration of protein binding (7.4 mg/g), and good reused properties. In the meantime, the GST-tagged GPX3 separated by these NSs can retain its redox state and peroxidase activity. Therefore, the prepared SnO2/SiO2-GSH NSs might find promising application in the rapid separation and purification of GST-tagged proteins.
Highlights
The easy separation and purification of proteins are very important in xenobiotic biotransformation, drug metabolism, biosynthesis of prostaglandins and steroid hormones, and degradation of aromatic amino acids [1,2,3,4,5,6]
Glutathione S-transferase (GST) represents a major group of detoxification isoenzymes which can be used in GST gene fusion system and medicine effect targeting field or as tumor markers [7, 8]
Various methods such as precipitation, chromatography, ultrafiltration, and dialysis are currently available for purifying various proteins, and in particular, affinity separation based on the natural biological affinity between biological macromolecules and complementary ligands is of extraordinary significance [9,10,11,12,13,14]
Summary
The easy separation and purification of proteins are very important in xenobiotic biotransformation, drug metabolism, biosynthesis of prostaglandins and steroid hormones, and degradation of aromatic amino acids [1,2,3,4,5,6]. Glutathione S-transferase (GST) represents a major group of detoxification isoenzymes which can be used in GST gene fusion system and medicine effect targeting field or as tumor markers [7, 8]. Various methods such as precipitation, chromatography, ultrafiltration, and dialysis are currently available for purifying various proteins, and in particular, affinity separation based on the natural biological affinity between biological macromolecules and complementary ligands is of extraordinary significance [9,10,11,12,13,14].
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