An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled β-amyloid peptide fragments Aβ (31-35), Aβ (1-40) and Aβ (1-42)

Xiaojun Ji; David Naistat; Changqing Li; Jhony Orbulescu; Roger M. Leblanc

doi:10.1016/j.colsurfb.2006.02.010

An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled β-amyloid peptide fragments Aβ (31-35), Aβ (1-40) and Aβ (1-42)

Xiaojun Ji, David Naistat, Changqing Li, Jhony Orbulescu, Roger M. Leblanc

Chemistry

Research output: Contribution to journal › Article

21 Scopus citations

Abstract

Aβ (31-35) peptide and control peptides as well as full length Aβ (1-40) and Aβ (1-42) peptides were labelled with luminescent CdSe/ZnS quantum dots (QDs) to observe the morphology of amyloid fibers. A comparison was made between QDs and an organic dye, namely Dansyl group, which showed that the QDs present a much better contrast for imaging than the organic dye.

Original language	English (US)
Pages (from-to)	104-111
Number of pages	8
Journal	Colloids and Surfaces B: Biointerfaces
Volume	50
Issue number	2
DOIs	https://doi.org/10.1016/j.colsurfb.2006.02.010
State	Published - Jul 1 2006

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Keywords

β-Amyloid peptide
Fluorescence imaging
Quantum dots

ASJC Scopus subject areas

Biotechnology
Colloid and Surface Chemistry
Physical and Theoretical Chemistry
Surfaces and Interfaces

Cite this

Ji, X., Naistat, D., Li, C., Orbulescu, J., & Leblanc, R. M. (2006). An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled β-amyloid peptide fragments Aβ (31-35), Aβ (1-40) and Aβ (1-42). Colloids and Surfaces B: Biointerfaces, 50(2), 104-111. https://doi.org/10.1016/j.colsurfb.2006.02.010

An alternative approach to amyloid fibrils morphology : CdSe/ZnS quantum dots labelled β-amyloid peptide fragments Aβ (31-35), Aβ (1-40) and Aβ (1-42). / Ji, Xiaojun; Naistat, David; Li, Changqing; Orbulescu, Jhony; Leblanc, Roger M.

In: Colloids and Surfaces B: Biointerfaces, Vol. 50, No. 2, 01.07.2006, p. 104-111.

Research output: Contribution to journal › Article

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Access to Document

10.1016/j.colsurfb.2006.02.010