Functionalization of α-synuclein Fibrils

Overview

Journal Beilstein J Nanotechnol

Specialty Biotechnology

Date 2015 Feb 12

PMID 25671157

Citations 4

Authors

Simona Poviloniene

Vida casaite

Virginijus Bukauskas

Arunas Setkus

Juozas Staniulis

Rolandas Meskys

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

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