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Enhanced Stability and Mechanical Properties of a Graphene-Protein Nanocomposite Film by a Facile Non-Covalent Self-Assembly Approach.


ABSTRACT: Graphene-based nanocomposite films (NCFs) are in high demand due to their superior photoelectric and thermal properties, but their stability and mechanical properties form a bottleneck. Herein, a facile approach was used to prepare nacre-mimetic NCFs through the non-covalent self-assembly of graphene oxide (GO) and biocompatible proteins. Various characterization techniques were employed to characterize the as-prepared NCFs and to track the interactions between GO and proteins. The conformational changes of various proteins induced by GO determined the film-forming ability of NCFs, and the binding of bull serum albumin (BSA)/hemoglobin (HB) on GO's surface was beneficial for improving the stability of as-prepared NCFs. Compared with the GO film without any additive, the indentation hardness and equivalent elastic modulus could be improved by 50.0% and 68.6% for GO-BSA NCF; and 100% and 87.5% for GO-HB NCF. Our strategy should be facile and effective for fabricating well-designed bio-nanocomposites for universal functional applications.

SUBMITTER: Du C 

PROVIDER: S-EPMC9000757 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature

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Enhanced Stability and Mechanical Properties of a Graphene-Protein Nanocomposite Film by a Facile Non-Covalent Self-Assembly Approach.

Du Chunbao C   Du Ting T   Zhou Joey Tianyi JT   Zhu Yanan Y   Jia Xingang X   Cheng Yuan Y  

Nanomaterials (Basel, Switzerland) 20220401 7


Graphene-based nanocomposite films (NCFs) are in high demand due to their superior photoelectric and thermal properties, but their stability and mechanical properties form a bottleneck. Herein, a facile approach was used to prepare nacre-mimetic NCFs through the non-covalent self-assembly of graphene oxide (GO) and biocompatible proteins. Various characterization techniques were employed to characterize the as-prepared NCFs and to track the interactions between GO and proteins. The conformationa  ...[more]

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