Insights on Aggregation of Hen Egg-White Lysozyme from Raman Spectroscopy and MD Simulations.

ABSTRACT: Protein misfolding and aggregation play a significant role in several neurodegenerative diseases. In the present work, the spontaneous aggregation of hen egg-white lysozyme (HEWL) in an alkaline pH 12.2 at an ambient temperature was studied to obtain molecular insights. The time-dependent changes in spectral peaks indicated the formation of β sheets and their effects on the backbone and amino acids during the aggregation process. Introducing iodoacetamide revealed the crucial role of intermolecular disulphide bonds amidst monomers in the aggregation process. These findings were corroborated by Molecular Dynamics (MD) simulations and protein-docking studies. MD simulations helped establish and visualize the unfolding of the proteins when exposed to an alkaline pH. Protein docking revealed a

SUBMITTER: Chalapathi D 

PROVIDER: S-EPMC9609503 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature