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

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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

Fingerprint

Synucleins
Intrinsically Disordered Proteins
Carbon Nanotubes
Single-walled carbon nanotubes (SWCN)
Carbon nanotubes
Proteins
Medical nanotechnology
Sonication
Functional materials
Polypeptides
Conformations
Peptides
Water

Keywords

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

Cite this

Chaudhary, Himanshu ; Fernandes, Ricardo M.F. ; Gowda, Vasantha ; Claessens, Mireille M.A.E. ; Furó, István ; Lendel, Christofer. / Intrinsically disordered protein as carbon nanotube dispersant : How dynamic interactions lead to excellent colloidal stability. In: Journal of colloid and interface science. 2019 ; Vol. 556. pp. 172-179.
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Intrinsically disordered protein as carbon nanotube dispersant : How dynamic interactions lead to excellent colloidal stability. / Chaudhary, Himanshu; Fernandes, Ricardo M.F.; Gowda, Vasantha; Claessens, Mireille M.A.E.; Furó, István; Lendel, Christofer.

In: Journal of colloid and interface science, Vol. 556, 15.11.2019, p. 172-179.

Research output: Contribution to journalArticleAcademicpeer-review

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AB - 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.

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