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Fibrillation inhibition investigated using micro- and nano scale Raman spectroscopy

7 Aug | By Volker Deckert
Fibrillation inhibition investigated using micro- and nano scale Raman spectroscopy
AFM topography image of insulin fibrils grown at pH 2.5 for 2.5 h in the presence of 100 μL of pure DMSO.
Image source: Image from Scientific Reports 6, Article number: 39622 (2016) doi:10.1038/srep39622

Fibril formation from native proteins has been associated with several neurodegenerative diseases. This renders the topic interesting for researchers of the Nanospectroscopy group at the Friedrich-Schiller-University and the Leibniz Institute of Photonic Technology Jena. 

A nanoscale molecular characterisation is beneficial to understand the fibrillation mechanism, as well as the dissection of fibrils. Tip-enhanced Raman scattering (TERS) was already employed to analyse amyloid fibrils chemically on a sub-protein basis. In this study, TERS is combined with conventional Raman spectroscopy and atomic force microscopy (AFM) to analyse Insulin assemblies that occurred during inhibition and dissection experiments in the presence of benzonitrile, dimethylsulfoxide, quercetin and β-carotene. 


Formation of bead-like insulin self-assemblies are indicated by the AFM topography. Raman and TERS measurements provide information on the secondary structure of bulk samples and single aggregates. TERS, due to its high spatial resolution is able to reveal surface conformations with the specific agents. Similar morphology but differing β-sheet structure content suggest different aggregation pathways, where the prevention of the β-sheet stacking of the peptide chains play a major role. Additionally to the amyloid-related research, the presented approach can also be applied to systems that require extremely surface-sensitive characterisation without the need of labels. 

Corresponding article in Scientific Reports

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