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Probing the fibrillation of lysozyme by nanoscale-infrared spectroscopy

journal contribution
submitted on 2024-05-14, 05:41 and posted on 2024-05-14, 05:42 authored by Zeyaul Islam, Mohamed H. Ali, Anton Popelka, Raghvendra Mall, Ehsan Ullah, Janarthanan Ponraj, Prasanna R. Kolatkar

Amyloid fibrillation is the root cause of several neuro as well as non-neurological disorders. Understanding the molecular basis of amyloid aggregate formation is crucial for deciphering various neurodegenerative diseases. In our study, we have examined the lysozyme fibrillation process using nano-infrared spectroscopy (nanoIR). NanoIR enabled us to investigate both structural and chemical characteristics of lysozyme fibrillar species concurrently. The spectroscopic results indicate that lysozyme transformed into a fibrillar structure having mainly parallel β-sheets, with almost no antiparallel β-sheets. Features such as protein stiffness have a good correlation with obtained secondary structural information showing the state of the protein within the fibrillation state. The structural and chemical details were compared with transmission electron microscopy (TEM) and circular dichroism (CD). We have utilized nanoIR and measured infrared spectra to characterize lysozyme amyloid fibril structures in terms of morphology, molecular structure, secondary structure content, stability, and size of the cross-β core. We have shown that the use of nanoIR can complement other biophysical studies to analyze the aggregation process and is particularly useful for studying proteins involved in aggregation to help in designing molecules against amyloid aggregation. Specifically, the nanoIR spectra afford higher resolution information and a characteristic fingerprint for determining states of aggregation.

Other Information

Published in: Journal of Biomolecular Structure and Dynamics
See article on publisher's website:



  • English


Taylor & Francis

Publication Year

  • 2020

License statement

This Item is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Institution affiliated with

  • Hamad Bin Khalifa University
  • Qatar Biomedical Research Institute - HBKU
  • Qatar Computing Research Institute - HBKU
  • Qatar Environment and Energy Research Institute - HBKU
  • Qatar University
  • Center for Advanced Materials - QU

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