Our current research focuses on the synthesis, purification, and characterization of 1,2-dithiolane modified self-assembling peptides. We have shown through past research that a peptide derived from the nucleating core of the peptide associated with Alzheimer’s disease can be modified at the N-terminus with a dithioester group and can self-assemble into supramolecular fibers. With confirmation of successful synthesis and characterization through the use of infrared spectroscopy, MALDI-TOF mass spectrometry, and TEM imaging analysis, we are now attempting to define the reactivity on the surfaces of a variety of supramolecular structures. We expect that like the nano-fibers that are formed from the peptide 1,2-dithioester-KVLFFAQ, nanotubes will form with the assembly of 1,2-dithioester-KLVFFAL. We will characterize the supramolecular reactivity by monitoring a thiol-thioester exchange reaction and other thiol-based chemistries. Additionally, MALDI mass imaging (MSI) analysis will also be used to create a 2D spatial image of heterogenous assemblies to determine if the modified 1,2-dithiolane self-assembling peptides co-assemble into one structure or self-sort into separate supramolecular structures. As chemists, the need to develop methods to better understand molecular interaction of multicomponent, heterogenous peptide assemblies is necessary in order to develop new peptide based biomaterials.

Exploring dynamic disulfide chemistry on supramolecular fibers

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.