Structural heterogeneities of self-assembled peptide nanomaterials

Neil R. Anthony; Anthony J. Bisignano; Anil K. Mehta; David G. Lynn; Keith M. Berland

doi:10.1117/12.909153

9 February 2012 Structural heterogeneities of self-assembled peptide nanomaterials

Neil R. Anthony, Anthony J. Bisignano, Anil K. Mehta, David G. Lynn, Keith M. Berland

Proceedings Volume 8226, Multiphoton Microscopy in the Biomedical Sciences XII; 82262U (2012) https://doi.org/10.1117/12.909153
Event: SPIE BiOS, 2012, San Francisco, California, United States

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.

Citation Download Citation

Neil R. Anthony, Anthony J. Bisignano, Anil K. Mehta, David G. Lynn, and Keith M. Berland "Structural heterogeneities of self-assembled peptide nanomaterials", Proc. SPIE 8226, Multiphoton Microscopy in the Biomedical Sciences XII, 82262U (9 February 2012); https://doi.org/10.1117/12.909153

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