Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability

Himanshu Chaudhary*, Ricardo M.F. Fernandes, Vasantha Gowda, Mireille M.A.E. Claessens, István Furó, Christofer Lendel

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
29 Downloads (Pure)

Abstract

The rich pool of protein conformations combined with the dimensions and properties of carbon nanotubes create new possibilities in functional materials and nanomedicine. Here, the intrinsically disordered protein α-synuclein is explored as a dispersant of single-walled carbon nanotubes (SWNTs) in water. We use a range of spectroscopic methods to quantify the amount of dispersed SWNT and to elucidate the binding mode of α-synuclein to SWNT. The dispersion ability of α-synuclein is good even with mild sonication and the obtained dispersion is very stable over time. The whole polypeptide chain is involved in the interaction accompanied by a fraction of the chain changing into a helical structure upon binding. Similar to other dispersants, we observe that only a small fraction (15–20%) of α-synuclein is adsorbed on the SWNT surface with an average residence time below 10 ms.

Original languageEnglish
Pages (from-to)172-179
Number of pages8
JournalJournal of colloid and interface science
Volume556
DOIs
Publication statusPublished - 15 Nov 2019

Keywords

  • Colloidal stability
  • Dispersibility
  • NMR
  • Noncovalent functionalization
  • SWNT
  • α-synuclein

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