| Literature DB >> 27734590 |
Qiqige Du1,2, Wanrong Li1, Ming Yuan1, Pei Gong1, Yi Zhang2, Feng Zhang1.
Abstract
Physisorptions occurs everywhere and constantly in living organisms and between nanomaterials and biomolecules. In this study, one of the most important proteins, G-actin, was selected to investigate its bio-nano physisorption with a model nanoparticle coated with a amphiphilic polymer. Using a photoluminescence quenching method, both the binding constant and the Hill constant were determined as 1.79 × 107 M-1 and 0.84, respectively. Thermodynamic calculations proved that such a physisorption was a spontaneous procedure. The physisorption-mediated protein-nanoparticle conjugates were robust enough to resist gel electrophoresis, and protein conformation was kept intact, as revealed using circular dichroism. This conjugate might be a promising candidate for nanofabrication or could play a significant role in actin-related bioactivities.Keywords: G-actin; amphiphilic polymer; binding constant; gold nanoparticle; photoluminescence quenching
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Year: 2016 PMID: 27734590 DOI: 10.1002/bio.3229
Source DB: PubMed Journal: Luminescence ISSN: 1522-7235 Impact factor: 2.464