In addition to its annual lectures, ChBE hosts a weekly seminar throughout the year with invited lecturers who are prominent in their fields. Unless otherwise noted, all seminars are held on Wednesdays in the Molecular Science and Engineering Building ("M" Building) in G011 (Cherry Logan Emerson Lecture Theater) at 4 p.m. Refreshments are served at 3:30 p.m. in the Emerson-Lewis Reception Salon.

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"Investigating Peptide and Protein Aggregation, Nanostructure Design and Structural Evolution with Solid State NMR"

Anant Paravastu, Associate Professor, Department of Chemical & Biomedical Engineering, Florida A&M University/Florida State University

Abstract:
Most proteins possess well-defined molecular structures stabilized by highly optimized interactions within chains of amino acids. Over the past decade, however, it has become clear that proteins and peptides (< 50 amino acids) can depart from their native structures and self-assemble into aggregates that are not uniquely specified by amino acid sequence. Aggregation can underlie pathology, as with amyloid diseases, but it can also be harnessed to produce beneficial nanomaterials such as artificial extracellular matrices. If we could understand pathological aggregation, we could design therapeutic strategies to control or prevent it. We could also design molecules to undergo specific self-assembly pathways. Towards these long-term goals, I will show how solid state NMR spectroscopy can be used to constrain molecular structural models of protein aggregates. My laboratory has applied this methodology to toxic oligomers of the Alzheimer’s β-amyloid peptide, a collection of human-designed self-assembling peptides, and aggregates of the naturally occurring β-trefoil protein fibroblast growth factor 1. Results will demonstrate that primary structure and environmental factors influence aggregation along specific pathways among energetically similar alternatives.