Protein Aggregation and Misfolding

The amyloid (misfolded) state of proteins and peptides is characterized by the formation of ordered aggregates with fibrous morphology and is linked to neurodegenerative diseases. 2D-IR spectroscopy along with residue specific isotope labeling can elucidate real time structural changes (intermediates) along aggregation pathways. Understanding these pathways will help in therapeutics targeting early stages of the diseases from fibril formations. Mechanistic insight of existing fibril inhibitors can also be obtained by studying the interactions and dynamics of the protein-inhibitor complexes.