Human Immune Protein C1q Selectively Disaggregates Carbon Nanotubes

Nano Lett. 2017 Jun 14;17(6):3409-3415. doi: 10.1021/acs.nanolett.7b00189. Epub 2017 May 30.

Abstract

We atomistically compute the change in free energy upon binding of the globular domain of the complement protein C1q to carbon nanotubes (CNTs) and graphene in solution. Our modeling results imply that C1q is able to disaggregate and disperse bundles of large diameter multiwalled CNTs but not those of thin single-walled CNTs, and we validate this prediction with experimental observations. The results support the view of a strong binding with potential implications for the understanding of the immune response and biomedical applications of graphitic nanomaterials.

Keywords: C1q; Carbon nanotubes; free energy; molecular dynamics; solvation; toxicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium / chemistry
  • Cations, Divalent
  • Collagen / chemistry
  • Complement C1q / chemistry*
  • Graphite / chemistry*
  • Humans
  • Molecular Dynamics Simulation
  • Nanotubes, Carbon / chemistry*
  • Particle Size
  • Protein Binding
  • Protein Conformation
  • Thermodynamics

Substances

  • Cations, Divalent
  • Nanotubes, Carbon
  • Graphite
  • Complement C1q
  • Collagen
  • Calcium