English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Influence of gold nanoparticles on the kinetics of α-synuclein aggregation.

Alvarez, Y. D., Fauerbach, J. A., Pellegrotti, J. V., Jovin, T. M., Jares-Erijman, E. A., & Stefani, F. D. (2013). Influence of gold nanoparticles on the kinetics of α-synuclein aggregation. Nano Letters, 13(12), 6156-6163. doi:10.1021/nl403490e.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-B39E-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-831B-7
Genre: Journal Article

Files

show Files
hide Files
:
1857732.pdf (Publisher version), 3MB
Name:
1857732.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://pubs.acs.org/doi/pdf/10.1021/nl403490e (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Alvarez, Y. D., Author
Fauerbach, J. A., Author
Pellegrotti, J. V., Author
Jovin, T. M.1, Author              
Jares-Erijman, E. A., Author
Stefani, F. D., Author
Affiliations:
1Emeritus Group Laboratory of Cellular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578629              

Content

show
hide
Free keywords: Gold nanoparticles, amyloid proteins, amyloid aggregation, Parkinson
 Abstract: α-synuclein (AS) is a small (140 amino acids), abundant presynaptic protein, which lacks a unique secondary structure in aqueous solution. Amyloid aggregates of AS in dopaminergic neurons of the midbrain are the hallmark of Parkinson’s disease (PD). The process of aggregation involves a series of complex structural transitions from innocuous monomeric AS to oligomeric, presumably neurotoxic, forms and finally to fibril formation. Despite its potential importance for understanding PD pathobiology and devising rational, targeted therapeutic strategies, the details of the aggregation process remain largely unknown. Methodologies and reagents capable of controlling the aggregation kinetics are essential tools for the investigation of the molecular mechanisms of amyloid diseases. In this work, we investigated the influence of citrate-capped gold nanoparticles on the aggregation kinetics of AS using a fluorescent probe (MFC) sensitive to the polarity of the molecular microenvironment via excited state intramolecular proton transfer (ESIPT). The particular effects on the half time, nucleation time, and growth rate were ascertained. Gold nanoparticles produced a strong acceleration of protein aggregation with an influence on both the nucleation and growth phases of the overall mechanism. The effects were dependent on the size and concentration of the nanoparticles, being strongest for nanoparticles 10 nm in diameter, which produced a 3-fold increase in the overall aggregation rate at concentrations as low as 20 nM.

Details

show
hide
Language(s): eng - English
 Dates: 2013-11-122013-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/nl403490e
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nano Letters
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 13 (12) Sequence Number: - Start / End Page: 6156 - 6163 Identifier: ISSN: 1530-6984
CoNE: /journals/resource/110978984570403