Article history: To elucidate the binding mechanism of graphene oxide (GO) with bovine serum albumin (BSA) at molec- Received 13 June 2017 ular level, it is urgent to investigate their interactions in this work. The results indicated that multi Received in revised form 1 August 2017 noncovalent forces including hydrophobic force, hydrogen bonds, van der Waals and -* stacking inter- Accepted 19 August 2017 actions were involved in the adsorption forces of BSA on GO surface. The kinetics of BSA adsorption onto Available online 25 August 2017 GO follows the pseudo-second-order kinetic model and was a fast process with high adsorption capacity. Some structure and functions of BSA were changed by GO binding. The decrease of melting tempera- Keywords: ture (T ) and enthalpy changes (H ) implied that BSA on GO surface is more prone towards thermal m m Graphene oxide denaturation. Drug competition experimental results showed that the binding afﬁnities of BSA with Bovine serum albumin 1-anilinonaphthalene-8-sulfonic acid (ANS) and oﬂoxacin (OFLX) were decreased to some extent. The Binding mechanism esterase-like activity of BSA was obviously increased and BSA became more glycosylated in the pres- Conformational change Activity ence of GO. Interestingly it was found that presence
Applied Surface Science – Elsevier
Published: Jan 1, 2018
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