ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Biphenyl ethers conjugated CdSe/ZnS core/shell quantum dots and interpretation of the mechanism of amyloid fibril disruption

Gupta, Sarika and Babu, Ponnusamy and Surolia, Avadhesha (2010) Biphenyl ethers conjugated CdSe/ZnS core/shell quantum dots and interpretation of the mechanism of amyloid fibril disruption. In: Biomaterials, 31 (26). pp. 6809-6822.

[img] PDF
ethens.pdf - Published Version
Restricted to Registered users only

Download (2502Kb) | Request a copy
Official URL: http://dx.doi.org/10.1016/j.biomaterials.2010.05.0...

Abstract

The biphenyl ethers (BPEs) are the potent inhibitors of TTR fibril formation and are efficient fibril disrupter. However, the mechanism by which the fibril disruption occurs is yet to be fully elucidated. To gain insight into the mechanism, we synthesized and used a new QD labeled BPE to track the process of fibril disruption. Our studies showed that the new BPE-QDs bind to the fiber uniformly and has affinity and specificity for TTR fiber and disrupted the pre-formed fiber at a relatively slow rate. Based on these studies we put forth the probable mechanism of fiber disruption by BPEs. Also, we show here that the BPE-QDs interact with high affinity to the amyloids of A beta(42), lysozyme and insulin. The potential of BPE-QDs in the detection of senile plaque in the brain of transgenic Alzheimer's mice has also been explored. (C) 2010 Elsevier Ltd. All rights reserved.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Transthyretin;Quantum Dots;Amyloidosis;Biphenyl ether; Amyloid
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 03 Sep 2010 11:13
Last Modified: 19 Sep 2010 06:15
URI: http://eprints.iisc.ernet.in/id/eprint/32003

Actions (login required)

View Item View Item