Suteewong, Teeraporn

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Suteewong, Teeraporn
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teeraporn.su@kmitl.ac.th

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    Item type:Publication,
    Controlled reversible assembly of gold nanoparticles as a new colorimetric and sensitive detection of glucose-6-phosphate dehydrogenase deficiency
    (2020-07-25)
    Boonyuen, Usa
    ;
    Praoparotai, Aun
    ;
    Chamchoy, Kamonwan
    ;
    Swangsri, Thitiluck
    ;
    Warakulwit, Chompunuch
    Recently, several studies have examined possible applications of nanoparticles for the development of electronic and optical sensors. The plasmon absorbance of gold nanoparticles has been used extensively to study biomolecular processes, including nicotinamide adenine dinucleotide/nicotinamide adenine dinucleotide phosphate-dependent enzymatic reactions. In this report, we describe the development of gold nanoparticles as a new colorimetric and sensitive detection method of glucose-6-phosphate dehydrogenase deficiency by means of controlled reversible assembly of gold nanoparticles. 3-nm polyvinylpyrrolidone/N,N′-dimethylaminopyridine-stabilized gold nanoparticles were synthesized, characterized and applied for an in vitro activity assay of 11 recombinant human glucose-6-phosphate dehydrogenase variants. Differences in the activity of the glucose-6-phosphate dehydrogenase variants from different deficiency classes were readily detected using the synthesized gold nanoparticles. The developed method can be easily distinguished with color change by naked eye for the detection of glucose-6-phosphate dehydrogenase deficiency. Moreover, we are the first to propose the segregation mechanism of polyvinylpyrrolidone/N,N′-dimethylaminopyridine-stabilized gold nanoparticles by reduced nicotinamide adenine dinucleotide phosphate. The method enables visual detection of glucose-6-phosphate dehydrogenase deficiency, which could be further developed for diagnostic testing of glucose-6-phosphate dehydrogenase deficiency.
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    Combined effects of double mutations on catalytic activity and structural stability contribute to clinical manifestations of glucose-6-phosphate dehydrogenase deficiency
    (2021-12-01)
    Pakparnich, Phonchanan
    ;
    Sudsumrit, Sirapapha
    ;
    Imwong, Mallika
    ;
    Suteewong, Teeraporn
    ;
    Chamchoy, Kamonwan
    Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common enzymopathy in humans, affecting ~ 500 million worldwide. A detailed study of the structural stability and catalytic activity of G6PD variants is required to understand how different mutations cause varying degrees of enzyme deficiency, reflecting the response of G6PD variants to oxidative stress. Furthermore, for G6PD double variants, investigating how two mutations jointly cause severe enzyme deficiency is important. Here, we characterized the functional and structural properties of nine G6PD variants: G6PD Gaohe, G6PD Mahidol, G6PD Shoklo, G6PD Canton, G6PD Kaiping, G6PD Gaohe + Kaiping, G6PD Mahidol + Canton, G6PD Mahidol + Kaiping and G6PD Canton + Kaiping. All variants were less catalytically active and structurally stable than the wild type enzyme, with G6PD double mutations having a greater impact than single mutations. G6PD Shoklo and G6PD Canton + Kaiping were the least catalytically active single and double variants, respectively. The combined effects of two mutations were observed, with the Canton mutation reducing structural stability and the Kaiping mutation increasing it in the double mutations. Severe enzyme deficiency in the double mutants was mainly determined by the trade-off between protein stability and catalytic activity. Additionally, it was demonstrated that AG1, a G6PD activator, only marginally increased G6PD enzymatic activity and stability.