Protein Misfolding Diseases ¨C Chemical, Mechanical, Structural and Biomimetics Perspective

Distinguished Lecture SeriesPresentsProfessor Ratnesh Lal,University of Chicago AbstractNative protein structures are determined by their primary sequences. Protein misfolding can lead normally folded soluble oligomers to form insoluble amyloid fibrils. In vivo, insoluble amyloid fibrils are linked to protein misfolding diseases, including Alzheimer¡¯s Disease (AD), Amyotrophic lateral sclerosis (ALS), prion-diseases, type-II diabetes and systemic amyloidosis. The mechanism of amyloid toxicity is poorly understood. Amyloid ¦Â peptide associated with Alzheimer¡¯s Disease forms a U-shaped ¡®¦Â-strand-turn-¦Â-strand¡¯ structure. Computational modeling based on protein folding energetics and mechanical mobility predicts these amyloids to form ion channels. Mutlimodal and mutlidimentional atomic force microscopy (AFM) study provides a new paradigm for amyloid diseases ¨C they belong to channelopathies and provide new avenues for designing therapeutics. This presentation will illustrate new advances in our understanding of amyloid diseases and will provide glimpse of biomimetics, bioMEMS, and other possible engineering approaches for effective diagnostics and therapy. Multiscale biomechanics covering nanoscale dissection, mechanics, rheology, cell micromechanics will also be discussed, in particular, using atomic force microscopy to study biological systems from single macromolecules to cell membrane to cells and tissue. We have obtained information about both their structures and their physiochemical properties with direct relevance to cell and tissue physiology, tissue mechanics, tissue remodeling, and biomimetics.

Location: SLH 100

Audiences: Everyone Is Invited

Contact: Petra Pearce Sapir