Interaction of Thermus thermophilus ArsC enzyme and gold nanoparticles naked-eye assays speciation between As(III) and As(V).
Nanotechnology
; 26(43): 435703, 2015 Oct 30.
Article
em En
| MEDLINE
| ID: mdl-26436536
ABSTRACT
The thermophilic bacterium Thermus thermophilus HB27 encodes chromosomal arsenate reductase (TtArsC), the enzyme responsible for resistance to the harmful effects of arsenic. We report on adsorption of TtArsC onto gold nanoparticles for naked-eye monitoring of biomolecular interaction between the enzyme and arsenic species. Synthesis of hybrid biological-metallic nanoparticles has been characterized by transmission electron microscopy (TEM), ultraviolet-visible (UV-vis), dynamic light scattering (DLS) and phase modulated infrared reflection absorption (PM-IRRAS) spectroscopies. Molecular interactions have been monitored by UV-vis and Fourier transform-surface plasmon resonance (FT-SPR). Due to the nanoparticles' aggregation on exposure to metal salts, pentavalent and trivalent arsenic solutions can be clearly distinguished by naked-eye assay, even at 85 µM concentration. Moreover, the assay shows partial selectivity against other heavy metals.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Arsênio
/
Proteínas de Bactérias
/
Thermus thermophilus
/
Arseniato Redutases
/
Nanopartículas Metálicas
/
Ouro
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article