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Reversible Lectin Binding to Glycan-Functionalized Graphene.

Tereza Koukalová1,2,3, Petr Kovaříček1,2, Pavla Bojarová3,4

  • 1J. Heyrovsky Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague, Czech Republic.

International Journal of Molecular Sciences
|July 2, 2021
PubMed
Summary
This summary is machine-generated.

Functionalizing graphene with chitooligomers enhances sensor selectivity for lectin proteins. This approach enables the development of specific carbohydrate-lectin binding sensors without compromising protein structure or function.

Keywords:
2D materialscarbohydrategraphenesensorwheat germ agglutinin

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Sensor Technology

Background:

  • Two-dimensional materials offer high sensitivity for sensors but lack selectivity.
  • Chemical functionalization is a key strategy to improve selectivity in 2D material-based sensors.

Purpose of the Study:

  • To develop a selective graphene-based sensor for detecting carbohydrate-protein interactions.
  • To functionalize graphene with chitooligomers to target specific lectin proteins.

Main Methods:

  • Graphene functionalization with a library of chitooligomers.
  • Characterization of grafted chitooligomers.
  • Studying glycan binding to wheat germ agglutinin using various methods.
  • Chemoenzymatic assay with horseradish peroxidase conjugate.

Main Results:

  • Successful grafting of chitooligomers onto graphene was confirmed.
  • High selectivity for lectin protein binding was achieved.
  • Protein quaternary structure remained intact after binding.
  • Lectin proteins could be released from the functionalized graphene surface.
  • Enzyme catalytic properties were preserved post-binding.

Conclusions:

  • Chitooligomer-functionalized graphene provides a selective platform for biosensing.
  • This method is suitable for developing sensitive and selective carbohydrate-lectin binding sensors.
  • The approach maintains the integrity and function of bound proteins.