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Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots

Paper ID Volume ID Publish Year Pages File Format Full-Text
10027 659 2010 8 PDF Available
Title
Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots
Abstract

One of the primary factors that induce Alzheimer's disease (AD) is the deposition of beta-amyloid (Aβ). The Aβ molecules can self-assemble to form neurotoxic aggregates with various morphologies, such as dimers, oligomers, protofibrils and fibrils. For this aspect, we demonstrated that the amyloid fibrillation can be inhibited by quenching the nucleation and elongation processes with a low concentration of water dispersed N-acetyl-l-cysteine capped quantum dots (NAC-QDs). Based on the concentration dependence of NAC-QDs on the seeded fibril growth, there is a remarkable inhibition effect when the NAC-QDs concentration is increased by 100-fold from 10−9 to 10−7 m. The NAC-QDs concentration required to show inhibition effect is much lower than that of the amyloid peptide concentration (50 μm). The step-like change suggests that the inhibition effect of NAC-QDs displays a threshold response. The inhibition is likely due to the intermolecular attractive interactions such as the hydrogen bonding between NAC-QDs and amyloid fibrils resulting in the blockage of the active elongation sites on the fibrils.

Keywords
Peptide; Self-assembly; TEM (transmission electron microscopy); Nanoparticle
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Inhibition of beta 1–40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 31, Issue 1, January 2010, Pages 91–98
Authors
, , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us