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Updated: May 13, 2026

Engineering Molecular Recognition with Bio-mimetic Polymers on Single Walled Carbon Nanotubes
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Lysozyme binds onto functionalized carbon nanotubes.

Francesca Bomboi1, Franco Tardani, Delia Gazzoli

  • 1Department of Physics, La Sapienza University, P.le A. Moro 5, I-00185 Rome, Italy.

Colloids and Surfaces. B, Biointerfaces
|March 26, 2013
PubMed
Summary
This summary is machine-generated.

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Single-walled carbon nanotubes interact with lysozyme, primarily through electrostatic forces. These interactions are pH-tunable and preserve the protein's native structure, offering insights into nanotube-protein conjugation.

Area of Science:

  • Nanotechnology
  • Biochemistry
  • Materials Science

Background:

  • Single-walled carbon nanotubes (SWCNTs) possess unique physicochemical properties.
  • Understanding SWCNT interactions with biological macromolecules like proteins is crucial for applications.
  • Specific studies on SWCNT-lysozyme interactions are needed to elucidate mechanisms.

Purpose of the Study:

  • To investigate the interaction mechanisms between oxidized SWCNTs and lysozyme.
  • To determine the effects of these interactions on lysozyme conformation.
  • To explore the influence of protein concentration and pH on conjugate formation.

Main Methods:

  • Formation of oxidized nanotube-lysozyme conjugates.
  • Analysis using electrophoretic mobility, dielectric spectroscopy, and dynamic light scattering.

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Dry Oxidation and Vacuum Annealing Treatments for Tuning the Wetting Properties of Carbon Nanotube Arrays
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Published on: April 15, 2013

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Last Updated: May 13, 2026

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Published on: January 10, 2017

Functionalization of Single-walled Carbon Nanotubes with Thermo-reversible Block Copolymers and Characterization by Small-angle Neutron Scattering
09:12

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08:59

Dry Oxidation and Vacuum Annealing Treatments for Tuning the Wetting Properties of Carbon Nanotube Arrays

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  • Assessment of protein secondary structure via circular dichroism.

    • Main Results:

    • Identified conditions for surface saturation of SWCNTs by lysozyme at various pH values.
    • Demonstrated that lysozyme largely retains its native secondary structure upon adsorption.
    • Confirmed that interactions are primarily electrostatic and pH-dependent.

    Conclusions:

    • Oxidized SWCNT-lysozyme interactions are predominantly electrostatic.
    • These interactions are tunable by adjusting solution pH.
    • Lysozyme maintains its native conformation when interacting with oxidized SWCNTs.