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Proceedings Paper

Structural heterogeneities of self-assembled peptide nanomaterials
Author(s): Neil R. Anthony; Anthony J. Bisignano; Anil K. Mehta; David G. Lynn; Keith M. Berland
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Paper Abstract

We use Fluorescence Lifetime Imaging Microscopy (FLIM) and Second Harmonic Imaging Microscopy (SHIM) to investigate the fundamental molecular mechanisms responsible for nucleation and growth of amyloidogenic-derived nanomaterials. The nanomaterials are assembled from of Amyloid-β(16-22), specifically Ac-KLVFFAE-NH2, the nucleating core of the Alzheimer's Amyloid-β protein. We describe how FLIM and SHIM can be used to follow different nucleation pathways and to quantify structural heterogeneities within these complex nanomaterials. New evidence suggests that different structures emerge from distinct nucleation pathways and these insights inform our understanding of the peptide self-assembly mechanisms. We discuss these insights in the context of a top down understanding of amyloidogenic diseases, the bottom up control of functional nanomaterials and the discovery of realtime structural indicators for nanofabrication strategies.

Paper Details

Date Published: 9 February 2012
PDF: 12 pages
Proc. SPIE 8226, Multiphoton Microscopy in the Biomedical Sciences XII, 82262U (9 February 2012); doi: 10.1117/12.909153
Show Author Affiliations
Neil R. Anthony, Emory Univ. (United States)
Anthony J. Bisignano, Emory Univ. (United States)
Anil K. Mehta, Emory Univ. (United States)
David G. Lynn, Emory Univ. (United States)
Keith M. Berland, Emory Univ. (United States)

Published in SPIE Proceedings Vol. 8226:
Multiphoton Microscopy in the Biomedical Sciences XII
Karsten König, Editor(s)

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