The supramolecular peptide self-assembly process presents new opportunities for the design and synthesis of dynamic and functional biomaterial-based systems. The self-assembly of peptides into cross-β supramolecular structures are largely driven by hydrophobic collapse and aggregation of peptides that contain a hydrophobic motif and the stabilization that arises from a network of amide backbone hydrogen bonds. With “design rules” for supramolecular assemblies in place, we are now focused on incorporating functional groups into self-assembling peptides such that those reactive groups can be accessed for post-assembly modification at the surface of the supramolecular structures. We report on the development of methods to assess supramolecular surface reactivity and functionalize supramolecular assemblies using a 1,2-dithiolane functional group. The amyloid Aβ derived peptide KLVFFAQ was modified with a 1,2-dithiolane group on the N-terminus and self-assembled into supramolecular nanofibers. Thiol reactivity at the supramolecular surface was induced by reducing agents and the reactivity was characterized by fluorescence, HPLC analysis and mass spectrometry. The long-term goal of this work is to provide fundamental knowledge on the molecular interactions and reactivity on supramolecular surfaces that are important in establishing new design rules for multicomponent and complex biomaterial-based systems. <br/>

Post-assembly surface reactivity of 1,2-dithiolane modified self-assembling peptides

2019 Spring National Meeting

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