Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability
[Display omitted] 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 nanot...
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Veröffentlicht in: | Journal of colloid and interface science 2019-11, Vol.556, p.172-179 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | [Display omitted]
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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ISSN: | 0021-9797 1095-7103 1095-7103 |
DOI: | 10.1016/j.jcis.2019.08.050 |