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A Redefined Protocol for Protein Corona Analysis on Graphene Oxide.

Asia Saorin1, Ahmed Subrati2, Alberto Martinez-Serra1

  • 1Department of Chemistry, Royal College of Surgeons in Ireland (RCSI), Dublin D02 YN77, Ireland.

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Summary

Standard methods for analyzing the protein corona on graphene oxide (GO) are insufficient. A new protocol using chaotropic agents improves protein recovery, revealing underestimated hydrophobic proteins and enhancing nanosafety studies.

Keywords:
graphene oxidenanosafetyprotein coronaprotein desorptionsurface interactions

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Area of Science:

  • Nanomaterials Science
  • Biomolecular Interactions
  • Analytical Chemistry

Background:

  • The biomolecular corona influences nanomaterial behavior, but characterization is challenging.
  • Graphene oxide (GO) presents unique properties affecting standard protein corona analysis.
  • Incomplete biomolecule recovery leads to biased results in nanosafety studies.

Purpose of the Study:

  • To identify limitations of standard protein elution methods for GO.
  • To develop an improved protocol for accurate protein corona characterization on GO.
  • To ensure reliable nanosafety assessments for advanced materials.

Main Methods:

  • Investigated limitations of SDS-based elution for graphene oxide (GO).
  • Developed and applied a novel stepwise elution protocol using chaotropic agents (urea, thiourea).
  • Compared protein recovery and composition between standard and modified methods.

Main Results:

  • Standard SDS-based methods underestimate strongly bound, hydrophobic proteins on GO.
  • The improved chaotropic agent protocol enables near-complete protein desorption.
  • Accurate characterization of the protein corona on GO is achievable with optimized methods.

Conclusions:

  • Existing protein elution protocols are inadequate for graphene oxide.
  • A chaotropic agent-based method enhances protein recovery and accuracy.
  • Optimized protocols are crucial for reliable nanosafety studies and sustainable material use.