A key problem in life-sciences research is to understand protein-protein interactions (PPI) with molecular and temporal resolution – this would allow the identification of the transient intermediates that play key roles in the function of biomacromolecular machines, signalling, translocation and folding to illuminate our understanding of disease development e.g. aberrant intracellular cell signalling in cancer and aggregation in amyloid disease. This presentation will outline the use of diazirines as powerful reagents to study β-sheet mediated PPIs specifically assembly of peptides into amyloid fibrils and will illustrate how, in combination with state-of the art mass-spectrometry, cross-linking encodes non-covalent structure in cross-linked peptides.<sup>1-2</sup> Alongside these studies, the presentation will outline how a suite of biochemical and computational methods can be harnessed to provide, for the first time, an analysis of the structural mechanism of surface-catalyzed secondary nucleation in amyloid assembly.<sup>3</sup>

Analysis of β-sheet mediated peptide assembly using a chemical biology approach

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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