About the event
Speaker: Ryanne Ballard, chemistry graduate student
Abstract: Organophosphorus toxicants (OP’s) have been known to inhibit Acetylcholinesterase (AChE), through widely accepted and proven mechanisms, leading to chronic illnesses and at times death. However, once AChE activity returns to basal levels, chronic illnesses can persist, lacking a defined mechanism not attributed to AChE inhibition. Recent studies have shown that exposure to these toxicants can result in OP adducts on lysine residues, and those in close proximity to glutamic acid residues, result in isopeptide crosslinking and protein aggregation. While the aggregation and isopeptide crosslinking have gained acceptance as possible origins of such chronic illnesses, the mechanism by which the crosslinking occurs remains conjectural. This presentation will discuss the synthetic methods by these vulnerable peptide sequences can by prepared, and their utility in probing this unknown mechanism through the use of liquid-phase peptide synthesis, 31P NMR, mass spectrometry, and high-pressure liquid chromatography.