This work was supported by the NSF (grant numbers 0932823, 0933384, and 0938019), the NIH (grant numbers 1R21CA121841-01A2 and 5R01EB007350-02), and in part by the DARPA (grant number W31P4Q-08-C-0426). S.I.Y. acknowledges the support of the Korea Research Foundation (grant number KRF-2008-357-D00078).
Communication
Inhibition of Amyloid Peptide Fibrillation by Inorganic Nanoparticles: Functional Similarities with Proteins†
Article first published online: 14 APR 2011
DOI: 10.1002/anie.201007824
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Yoo, S. I., Yang, M., Brender, J. R., Subramanian, V., Sun, K., Joo, N. E., Jeong, S.-H., Ramamoorthy, A. and Kotov, N. A. (2011), Inhibition of Amyloid Peptide Fibrillation by Inorganic Nanoparticles: Functional Similarities with Proteins. Angew. Chem. Int. Ed., 50: 5110–5115. doi: 10.1002/anie.201007824
- †
Publication History
- Issue published online: 16 MAY 2011
- Article first published online: 14 APR 2011
- Manuscript Received: 12 DEC 2010
Funded by
- NSF. Grant Numbers: 0932823, 0933384, 0938019
- NIH. Grant Numbers: 1R21CA121841-01A2, 5R01EB007350-02
- DARPA. Grant Number: W31P4Q-08-C-0426
- Korea Research Foundation. Grant Number: KRF-2008-357-D00078
Keywords:
- fibrils;
- nanoparticles;
- peptides;
- self-assembly

Nanoparticles for amyloid diseases: CdTe nanoparticles (NPs) can efficiently prevent fibrillation of amyloid peptides; the process is based on the multiple binding of Aβ oligomers to CdTe NPs. The molar efficiency and the inhibition mechanism displayed by the NPs are analogous to the mechanism found for proteins responsible for the prevention of amyloid fibrillation in the human body.

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