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Methods to Characterize the Nanostructure and Molecular Organization of Amphiphilic Peptide Assemblies

  • V. CastellettoEmail author
  • I. W. HamleyEmail author
Protocol
First Online:
Part of the Methods in Molecular Biology book series (MIMB, volume 1777)

Abstract

Methods to characterize the nanostructure and molecular organization of aggregates of peptides such as amyloid or amphiphilic peptide assemblies are reviewed. We discuss techniques to characterize conformation and secondary structure including circular and linear dichroism and FTIR and Raman spectroscopies, as well as fluorescence methods to detect aggregation. NMR spectroscopy methods, especially solid-state NMR measurements to probe beta-sheet packing motifs, are also briefly outlined. Also discussed are scattering methods including X-ray diffraction and small-angle scattering techniques including SAXS (small-angle X-ray scattering) and SANS (small-angle neutron scattering) and dynamic light scattering. Imaging methods are direct methods to uncover features of peptide nanostructures, and we provide a summary of electron microscopy and atomic force microscopy techniques. Selected examples are highlighted showing data obtained using these techniques, which provide a powerful suite of methods to probe ordering from the molecular scale to the aggregate superstructure.

Key words

Peptides Conformation Secondary structure Characterization methods X-ray diffraction Fluorescence spectroscopy Circular dichroism Linear dichroism FTIR spectroscopy NMR Light scattering Small-angle X-ray scattering (SAXS) Small-angle neutron scattering (SANS) Atomic force microscopy (AFM) Electron microscopy 
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Notes

Acknowledgements

This work was supported by EPSRC Platform Grant reference EPSRC EP/L020599/1. We thank our collaborators for their vital contributions to several aspects of our ongoing research, especially in the fields of AFM imaging (Prof Raffaele Mezzenga and Dr. Jozef Adamcik, ETH Zürich) and cryo-TEM imaging (Prof Janne Ruokolainen and his team at Aalto University, Finland).

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© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of ReadingReadingUK

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