DataVXSmallPaper
journal article·2015-09Open access

Amyloid Fibrils: Nanoscale Heterogeneity of the Molecular Structure of Individual hIAPP Amyloid Fibrils Revealed with Tip‐Enhanced Raman Spectroscopy (Small 33/2015)

Corianne C. vandenAkker, Tanja Deckert‐Gaudig, Michael Schleeger, Krassimir P. Velikov, Volker Deckert, Mischa Bonn, Gijsje H. Koenderink

Small· Volume 11· Issue 33
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Source abstract

Abstract

Many diseases, including type 2 diabetes, are linked to the pathological deposition of nanoscale, fibrillar protein aggregates called amyloids. Since the surface of amyloid fibrils plays a key role in amyloid toxicity and membrane damage, knowledge of the surface structure is essential. On page 4131, V. Deckert, G. H. Koenderink, and co-workers probe the molecular structure and amino acid residue composition with tipenhanced Raman spectroscopy. The surface of amyloid fibrils contains mainly unstructured or α-helical structures, in contrast to the core, which is dominated by β-sheets.
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Research context

NanomaterialsMaterials processing

OpenAlex topics: Alzheimer's disease research and treatments

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Affiliations

FOM Institute AMOLF Science Park 104 1098 XG Amsterdam The Netherlands

Leibniz Institute of Photonic Technology Albert‐Einstein‐Straße 9 07745 Jena Germany

Department of Molecular Spectroscopy Max Planck Institute for Polymer Research Ackermannweg 10 55128 Mainz Germany

Soft Condensed Matter Debye Institute for Nanomaterials Science Department of Physics and Astronomy Utrecht University Princetonplein 5 3584 CC Utrecht The Netherlands

Unilever Research Labs NL‐3133 AT Vlaardingen The Netherlands

Institute for Physical Chemistry and Abbe Center of Photonics University of Jena Helmholtzweg 4 07743 Jena Germany

References

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