Functionalization of α-synuclein fibrils
The propensity of peptides and proteins to form self-assembled structures has very promising applications in the development of novel nanomaterials. Under certain conditions, amyloid protein α-synuclein forms well-ordered structures – fibrils, which have proven to be valuable building blocks for bio...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Beilstein-Institut
2015-01-01
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| Series: | Beilstein Journal of Nanotechnology |
| Subjects: | |
| Online Access: | https://doi.org/10.3762/bjnano.6.12 |
| Summary: | The propensity of peptides and proteins to form self-assembled structures has very promising applications in the development of novel nanomaterials. Under certain conditions, amyloid protein α-synuclein forms well-ordered structures – fibrils, which have proven to be valuable building blocks for bionanotechnological approaches. Herein we demonstrate the functionalization of fibrils formed by a mutant α-synuclein that contains an additional cysteine residue. The fibrils have been biotinylated via thiol groups and subsequently joined with neutravidin-conjugated gold nanoparticles. Atomic force microscopy and transmission electron microscopy confirmed the expected structure – nanoladders. The ability of fibrils (and of the additional components) to assemble into such complex structures offers new opportunities for fabricating novel hybrid materials or devices. |
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| ISSN: | 2190-4286 |