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

doi:10.1016/j.jcis.2019.08.050

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

J Colloid Interface Sci. 2019 Nov 15:556:172-179. doi: 10.1016/j.jcis.2019.08.050. Epub 2019 Aug 14.

Authors

Himanshu Chaudhary¹, Ricardo M F Fernandes², Vasantha Gowda³, Mireille M A E Claessens⁴, István Furó³, Christofer Lendel⁵

Affiliations

¹ Department of Chemistry, Division of Applied Physical Chemistry, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden. Electronic address: himcha@kth.se.
² Department of Chemistry, Division of Applied Physical Chemistry, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden; Centro de Investigação em Química, Department of Chemistry and Biochemistry, Faculty of Science, University of Porto, Rua do Campo Alegre, s/n, P-4169-007 Porto, Portugal. Electronic address: rmff@kth.se.
³ Department of Chemistry, Division of Applied Physical Chemistry, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden.
⁴ MESA + Institute for Nanotechnology and Mira Institute for Biomedical Technology and Technical Medicine, University of Twente, 7500AE Enschede, the Netherlands.
⁵ Department of Chemistry, Division of Applied Physical Chemistry, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden. Electronic address: lendel@kth.se.

PMID: 31445446
DOI: 10.1016/j.jcis.2019.08.050

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.

Keywords: Colloidal stability; Dispersibility; NMR; Noncovalent functionalization; SWNT; α-synuclein.

MeSH terms

Colloids
Humans
Intrinsically Disordered Proteins / chemistry*
Nanotubes, Carbon / chemistry*
alpha-Synuclein / chemistry*

Substances

Colloids
Intrinsically Disordered Proteins
Nanotubes, Carbon
SNCA protein, human
alpha-Synuclein