Probing the fibrillation of lysozyme by nanoscale-infrared spectroscopy.

Journal of Biomolecular Structure & Dynamics
Zeyaul IslamPrasanna R Kolatkar

Abstract

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 pa...Continue Reading

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Citations

Mar 16, 2021·Journal of Biomolecular Structure & Dynamics·Mouhi Eddine HachimMy Youssef Ait Itto
Oct 13, 2021·Physical Chemistry Chemical Physics : PCCP·Antonio Francés-MonerrisMarco Marazzi

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Methods Mentioned

BETA
protein folding
atomic force microscopy
infrared spectroscopy
transmission
circular dichroism
AFM
PCA

Software Mentioned

plot3D
stats
A2R
R
A2R A2R
Origin PRO
Anasys
CONTIN
factoextra

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