Changing the activities and structures of bovine serum albumin bound to graphene oxide

Changing the activities and structures of bovine serum albumin bound to graphene oxide 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Surface Science Elsevier

Changing the activities and structures of bovine serum albumin bound to graphene oxide

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier B.V.
ISSN
0169-4332
eISSN
1873-5584
D.O.I.
10.1016/j.apsusc.2017.08.130
Publisher site
See Article on Publisher Site

Abstract

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

Journal

Applied Surface ScienceElsevier

Published: Jan 1, 2018

References

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