Nano-size dependence in the adsorption by the SARS-CoV-2 spike protein over gold colloid.
Colloids Surf A Physicochem Eng Asp
; 615: 126275, 2021 Apr 20.
Article
em En
| MEDLINE
| ID: mdl-33564211
ABSTRACT
Gold nano-particles were coated with the spike protein (S protein) of SARS-CoV-2 and exposed to increasingly acidic conditions. Their responses were investigated by monitoring the surface plasmon resonance (SPR) band shift. As the external pH was gradually changed from neutral pH to pH â¼2 the peak of the SPR band showed a significant red-shift, with a sigmoidal feature implying the formation of the gold-protein aggregates. The coating of S protein changed the surface property of the gold enough to extract the coverage fraction of protein over nano particles, Θ, which did not exhibit clear nano-size dependence. The geometrical simulation to explain Θ showed the average axial length to be a = 7. 25 nm and b =8.00 nm when the S-protein was hypothesized as a prolate shape with spiking-out orientation. As the pH value externally hopped between pHâ¼3 and pHâ¼10, a behavior of reversible protein folding was observed for particles with diameters >30 nm. It was concluded that S protein adsorption conformation was impacted by the size (diameter, d) of a core nano-gold, where head-to-head dimerized S protein was estimated for d ≤ 80 nm and a parallel in opposite directions formation for d = 100 nm.
ACE2, Angiotensin Converting Enzyme; CoV-2, Corona Virus 2; Gold nano-particles; Protein folding; RBD, receptor binding domain; Reversible self-assembly; S protein, Spike protein; SARS, Severe Acute Respiratory Syndrome; SARS-CoV-2; SPR (surface plasmon resonance) band; Spike protein; TMPRSS2, Transmembrane protease serine 2
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Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Colloids Surf A Physicochem Eng Asp
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Estados Unidos