Neuronal protein aggregation has been implicated in several neurodegenerative diseases. In particular, misfolding of proteins such as beta-amyloids and alpha-synuclein are known to lead to diseases such as Alzheimer’s and Parkinson’s diseases. In fact, recent studies have revealed the inter-play of these proteins in both diseases. In this work, we investigated the binding interactions of a series of polyphenols and sesquiterpenoids as well as their peptide derivatives with alpha-synulclein and beta-amyloid peptides. In addition to docking studies and protein-ligand profiler studies we carried out extensive molecular dynamics studies to examine the stability of the ligand bound proteins. MMGBSA analyses were also carried out. In addition to in-silico studies, CD spectroscopy and fluorescence analysis revealed that in most cases the peptide bound derivatives significantly enhanced interactions and mitigated beta-sheet formation.

Interactions of neuronal proteins with sesquiterpenoids and polyphenols

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.