Protein misfolding and aggregation is a key attribute of different neurodegenerative diseases.
Misfolded and aggregated proteins are intrinsically disordered and rule out structure based
drug design. The comprehensive characterization of misfolded proteins and associated aggregation
pathway is prerequisite to develop therapeutics for neurodegenerative diseases caused due to the
protein aggregation. Visible protein aggregates used to be the final stage during aggregation mechanism.
The structural analysis of intermediate steps in such protein aggregates will help us to discern
the conformational role and subsequently involved pathways. The structural analysis of protein aggregation
using various biophysical methods may aid for improved therapeutics for protein misfolding
and aggregation related neurodegenerative diseases. In this mini review, we have summarized
different spectroscopic methods such as fluorescence spectroscopy, circular dichroism (CD), nuclear
magnetic resonance (NMR) spectroscopy, Fourier transform infrared spectroscopy (FTIR), and Raman
spectroscopy for structural analysis of protein aggregation. We believe that the understanding of
invisible intermediate of misfolded proteins and the key steps involved during protein aggregation
mechanisms may advance the therapeutic approaches for targeting neurological diseases that are
caused due to misfolded proteins.
Keywords: Neurodegenerative diseases, protein aggregation, NMR spectroscopy, fluorescence spectroscopy, amyloid like proteins,
circular dichroism, raman spectroscopy.
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